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evolution
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enzyme HP-NAP belongs to the DNA-protecting proteins under starved conditions (Dps) family, which has significant structural similarities to the dodecameric ferritin family. The overall structure of HP-NAP YS39 is similar to those of other HP-NAPs and Dps proteins
evolution
in addition to the classical classification, another cluster containing AaMco1 and filamentous ascomycete hypothetical proteins, putative multicopper oxidases (MCOs) or proteins called ascorbate oxidases is identified on the basis of sequence similarity. This group is named ascomycete MCOs. Neighbor joining tree of multicopper oxidase amino acid sequences, phylogenetic analysis, overview
evolution
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the ferritin (Ftn) and bacterioferritin (Bfr) proteins of the ferritin-like superfamily constitute a prime example of a remarkable combination of evolutionary conserved iron uptake and release processes that are integrated with a variety in iron translocation mechanisms. Ftns and Bfrs have a highly conserved architecture
evolution
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the ferritin (Ftn) and bacterioferritin (Bfr) proteins of the ferritin-like superfamily constitute a prime example of a remarkable combination of evolutionary conserved iron uptake and release processes that are integrated with a variety in iron translocation mechanisms. Ftns and Bfrs have a highly conserved architecture
evolution
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enzyme HP-NAP belongs to the DNA-protecting proteins under starved conditions (Dps) family, which has significant structural similarities to the dodecameric ferritin family. The overall structure of HP-NAP YS39 is similar to those of other HP-NAPs and Dps proteins
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evolution
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in addition to the classical classification, another cluster containing AaMco1 and filamentous ascomycete hypothetical proteins, putative multicopper oxidases (MCOs) or proteins called ascorbate oxidases is identified on the basis of sequence similarity. This group is named ascomycete MCOs. Neighbor joining tree of multicopper oxidase amino acid sequences, phylogenetic analysis, overview
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malfunction
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cytosolic FOX activity increases 30% in iron-deficient rats (compared with controls) but is unchanged in copper-deficient rats
malfunction
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knockdown of MCO1 is correlated with increased longevity on high-iron food and decreased iron accumulation
malfunction
strongly pronounced argyrosis caused by adding AgCl to the feed of laboratory rats efficiently mimics the deficiency of ceruloplasmin ferroxidase activity. The deficiency of ceruloplasmin ferroxidase activity in Ag-fed rats affects the iron content in serum, though does not prevent the recovery of hemoglobin level accompanied by exhaustion of iron caches in liver and spleen. When apolactoferrin (apo-LF) is administered to Ag-rats suffering from either post-hemorrhagic or hemolytic anemia, both hemoglobin and serum iron are restored more rapidly than in the control animals. Saturation of apo-LF with iron, provided by active ceruloplasmin, can strongly affect its protective capacity. Phenotype, overview
malfunction
deletion of the rv0846c gene increases the susceptibility of Mycobacterium tuberculosis to copper at least 10fold
malfunction
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deletion of the rv0846c gene increases the susceptibility of Mycobacterium tuberculosis to copper at least 10fold
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malfunction
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strongly pronounced argyrosis caused by adding AgCl to the feed of laboratory rats efficiently mimics the deficiency of ceruloplasmin ferroxidase activity. The deficiency of ceruloplasmin ferroxidase activity in Ag-fed rats affects the iron content in serum, though does not prevent the recovery of hemoglobin level accompanied by exhaustion of iron caches in liver and spleen. When apolactoferrin (apo-LF) is administered to Ag-rats suffering from either post-hemorrhagic or hemolytic anemia, both hemoglobin and serum iron are restored more rapidly than in the control animals. Saturation of apo-LF with iron, provided by active ceruloplasmin, can strongly affect its protective capacity. Phenotype, overview
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metabolism
the initial step in the iron store mechanism occurs when the Fe(II) is oxidize to Fe(III) at the ferroxidase center (FC) found in the H-chain from mammalian ferritins, bacterial ferritins and Bfr subunits
metabolism
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the initial step in the iron store mechanism occurs when the Fe(II) is oxidize to Fe(III) at the ferroxidase center (FC) found in the H-chain from mammalian ferritins, bacterial ferritins and Bfr subunits
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physiological function
binding and oxidization of iron, thus preventing the formation of harmful reactive oxygen species
physiological function
essential to iron homeostasis in green algae
physiological function
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FOX1 is important for iron uptake in a situation of iron deficiency
physiological function
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iron provoked inhibition of osteoblast activity leading to osteoporosis and osteopenia is mediated by ferritin and its ferroxidase activity
physiological function
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stores iron as a hydrous ferric oxide mineral core within a shell-like structure of 4/3/2 octahedral symmetry
physiological function
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Dps proteins contain a ferroxidase site that binds and oxidizes iron, thereby consuming H2O2 and preventing hydroxyl radical formation by Fenton reaction. Dps proteins oxidize Fe2+ to Fe3+ using 12 ferroxidase centers, each of them located at a dimer interface
physiological function
Thermosynechococcus vestitus
DpsA-Te can protect DNA molecules against Fe(II)-mediated and H2O2-mediated damage. Dps-Te and DpsA-Te, together with ferritin, play an important role in alleviating the toxic effects of reactive oxygen species, physiological basis of the coexistence of two Dps proteins in the organism, overview
physiological function
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ferritin is a ubiquitous iron-storage protein that has 24 subunits. Each subunit of ferritins that exhibit high Fe2+ oxidation rates has a diiron binding site, the socalled ferroxidase center. The role of the ferroxidase center appears to be essential for the iron-oxidation catalysis of ferritins
physiological function
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native function includes the interaction with the iron permease, Ftr1p, and wild-type high-affinity iron uptake activity. The four essential sequons are found within relatively nonpolar regions located in surface recesses and are strongly conserved among fungal Fet3 proteins
physiological function
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the non-heme iron-binding ferritin with dual ferroxidase and DNA-binding functionality reported herein, may play a significant urease-independent role in the acid adaptation of Helicobacter pylori under physiological conditions in vivo
physiological function
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the two ferroxidases are likely involved in high-affinity Fe-uptake in Candida albicans, Fet31 and Fet34, both support Fe-uptake along with an Ftr1 protein, either from Candida albicans or from Saccharomyces cerevisiae. CaFtr1 and not CaFtr2 is required for the virulence of the pathogen
physiological function
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ceruloplasmin is one of the most complex multicopper oxidase enzymes and plays an essential role in the metabolism of iron in mammals. Ferrous ion supplied by the ferroportin exporter is converted by ceruloplasmin to ferric ion that is accepted by plasma metallo-chaperone transferrin. The multicopper oxidase enzymes mediate transfer of the iron from the cell export pump ferroportin to the plasma metallo-chaperone transferrin. Specifically, they are responsible for conversion of Fe(II) to Fe(III), the form in which it is transported in the blood by transferrin
physiological function
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ceruloplasmin's primary physiological role in the association of plasma redox reactions
physiological function
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ferritin and ferritin-like molecules (Bfr and bacterial Ftn) are supramolecular assemblies built from 24 subunits into a nearly spherical architecture with a hollow core where up to 4000 iron ions can be stored as a ferric mineral that is protected from indiscriminant cellular reducing agents. The enzymes possess an integrated ferroxidase activity, EC 1.16.3.1. Network-weaving algorithm that passes threads of an allosteric network through highly correlated residues using hierarchical clustering, the residue-residue correlations are calculated, modeling, overview. Each type of ferritin-like molecule has an extended network of highly correlated residues, connecting distant pores and the ferroxidase center. The ferritin structures evolved in a way to limit the influence of functionally unrelated events in the cytoplasm on the allosteric network to maintain stability of the translocation mechanisms. Diversity in mechanisms of iron traffic, overview. It is thought that iron translocation across the ferritin shell requires cooperative motions of residues aligning the path. In the process of iron capture and storage, iron traverses from the ferritin exterior surface to the interior cavity via a ferroxidase center, where soluble Fe2+ is oxidized to Fe3+. A ferroxidase center is located in the middle of each subunit in Bfrs. Release of iron from the ferritin cavity requires reduction of ferric iron in the interior ferritin cavity and egress of ferrous ions via pores in the protein shell. The networks in BfrB and FtnA connect the ferroxidase center with the 4fold pores and B-pores, leaving the 3fold pores unengaged
physiological function
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ferritin and ferritin-like molecules (Bfr and bacterial Ftn) are supramolecular assemblies built from 24 subunits into a nearly spherical architecture with a hollow core where up to 4000 iron ions can be stored as a ferric mineral that is protected from indiscriminant cellular reducing agents. The enzymes possess an integrated ferroxidase activity, EC 1.16.3.1. Network-weaving algorithm that passes threads of an allosteric network through highly correlated residues using hierarchical clustering, the residue-residue correlations are calculated, modeling, overview. Each type of ferritin-like molecule has an extended network of highly correlated residues, connecting distant pores and the ferroxidase center. The ferritin structures evolved in a way to limit the influence of functionally unrelated events in the cytoplasm on the allosteric network to maintain stability of the translocation mechanisms. Diversity in mechanisms of iron traffic, overview. It is thought that iron translocation across the ferritin shell requires cooperative motions of residues aligning the path. In the process of iron capture and storage, iron traverses from the ferritin exterior surface to the interior cavity via a ferroxidase center, where soluble Fe2+ is oxidized to Fe3+. A ferroxidase center is located in the middle of each subunit in bacterial Ftn. Release of iron from the ferritin cavity requires reduction of ferric iron in the interior ferritin cavity and egress of ferrous ions via pores in the protein shell. The networks in BfrB and FtnA connect the ferroxidase center with the 4fold pores and B-pores, leaving the 3fold pores unengaged
physiological function
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ferritin and ferritin-like molecules (Bfr and bacterial Ftn) are supramolecular assemblies built from 24 subunits into a nearly spherical architecture with a hollow core where up to 4000 iron ions can be stored as a ferric mineral that is protected from indiscriminant cellular reducing agents. The enzymes possess an integrated ferroxidase activity, EC 1.16.3.1. Network-weaving algorithm that passes threads of an allosteric network through highly correlated residues using hierarchical clustering, the residue-residue correlations are calculated, modeling, overview. The ferritin structures evolved in a way to limit the influence of functionally unrelated events in the cytoplasm on the allosteric network to maintain stability of the translocation mechanisms. Diversity in mechanisms of iron traffic, overview. It is thought that iron translocation across the ferritin shell requires cooperative motions of residues aligning the path. In the process of iron capture and storage, iron traverses from the ferritin exterior surface to the interior cavity via a ferroxidase center, where soluble Fe2+ is oxidized to Fe3+. A ferroxidase center is located in the middle of each subunit in the heavy (H)-type and M-type subunits of eukaryotic Ftns. Release of iron from the ferritin cavity requires reduction of ferric iron in the interior ferritin cavity and egress of ferrous ions via pores in the protein shell. The networks in BfrB and FtnA connect the ferroxidase center with the 4fold pores and B-pores, leaving the 3fold pores unengaged
physiological function
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ferritins are iron-storage nanocage proteins that catalyze the oxidation of Fe2+ to Fe3+ at ferroxidase sites. Ferroxidase activity in eukaryotic ferritin is controlled by accessory-iron-binding sites in the catalytic cavity, a ferroxidase-active cage, overview
physiological function
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ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
physiological function
ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
physiological function
ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
physiological function
ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
physiological function
ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
physiological function
ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
physiological function
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neutrophil-activating protein (HP-NAP) is one of a number of virulence factors in Helicobacter pylori. The enzyme promote the adhesion of neutrophils to endothelial cells, and activates NADPH oxidase to produce reactive oxygen species via a cascade of intracellular activation events. HP-NAP binds to the outer membrane surface, which mediates binding to mucin or glycosphingolipids. This protein can also stimulate the production of tissue factor and plasminogen activator inhibitor-2 by human monocytes. HP-NAP can cross the endothelium to promote neutrophil adhesion in vivo and can activate the underlying mast cells. HP-NAP stimulates Th1 immune responses by inducing the production of cytokines, such as interleukin-12 (IL-12) and IL-23. HP-NAP is a major antigen in the immune response to Helicobacter pylori infections. HP-NAP protects Helicobacter pylori from iron-mediated oxidative DNA damage by sequestering free iron, similar to Dps proteins, which protect DNA from oxidative damage
physiological function
the recombinant Chlorobium tepidum ferritin (rCtFtn) is able to oxidize iron with a moderate ferroxidase activity
physiological function
multicopper oxidase is required for copper resistance in Mycobacterium tuberculosis
physiological function
the enzyme is required for iron homeostasis. It also plays a major role in maintaining the cuprous/cupric redox balance
physiological function
the enzyme is required for iron homeostasis. It also plays a major role in maintaining the cuprous/cupric redox balance
physiological function
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neutrophil-activating protein (HP-NAP) is one of a number of virulence factors in Helicobacter pylori. The enzyme promote the adhesion of neutrophils to endothelial cells, and activates NADPH oxidase to produce reactive oxygen species via a cascade of intracellular activation events. HP-NAP binds to the outer membrane surface, which mediates binding to mucin or glycosphingolipids. This protein can also stimulate the production of tissue factor and plasminogen activator inhibitor-2 by human monocytes. HP-NAP can cross the endothelium to promote neutrophil adhesion in vivo and can activate the underlying mast cells. HP-NAP stimulates Th1 immune responses by inducing the production of cytokines, such as interleukin-12 (IL-12) and IL-23. HP-NAP is a major antigen in the immune response to Helicobacter pylori infections. HP-NAP protects Helicobacter pylori from iron-mediated oxidative DNA damage by sequestering free iron, similar to Dps proteins, which protect DNA from oxidative damage
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physiological function
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ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
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physiological function
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ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
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physiological function
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ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
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physiological function
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the enzyme is required for iron homeostasis. It also plays a major role in maintaining the cuprous/cupric redox balance
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physiological function
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multicopper oxidase is required for copper resistance in Mycobacterium tuberculosis
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physiological function
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FOX1 is important for iron uptake in a situation of iron deficiency
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physiological function
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the recombinant Chlorobium tepidum ferritin (rCtFtn) is able to oxidize iron with a moderate ferroxidase activity
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physiological function
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ferroxidase-mediated iron oxide biomineralization. The formation of iron-oxo particles in all these compartments requires a series of steps including recruitment of iron, translocation, oxidation, nucleation, and storage, that are mediated by ferroxidase centers. Compartmentalized iron oxide biomineralization yields uniform nanoparticles strictly determined by the sizes of the compartments. Dps, ferritin, and encapsulin all form protein-coated minerals of variable small sizes with similar iron oxide composition
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additional information
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core glycosylation suppresses Fet3p nascent chain aggregation during synthesis into the endoplasmic reticulum. Fet3 protein lacking any one of the glycan units is found in an intracellular high-molecular mass species. But the missing carbohydrate is not required for native structure and biologic activity
additional information
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Dps-like, i.e. DNA-binding protein from starved cells-like, proteins belong to the ferritin superfamily. They form 12-mers instead of 24-mers, in contrast to ferritins, and have a different ferroxidase center, and are able to store a smaller amount of about 500 iron atoms in a hollow cavity
additional information
Thermosynechococcus vestitus
DpsA-Te ows a unique substitution of a metal ligand at the A-site, i.e. His78 in place of the canonical Asp, and a His164 in place of a hydrophobic residue at a metal-coordinating distance in the B-site. In contrast to the typical behavior of Dps proteins, where Fe2+ oxidation by H2O2 is about 100fold faster than by O2, in DpsA-Te the ferroxidation efficiency of O2 is very high and resembles that of H2O2. DpsA-Te contains two Zn2+ bound at the ferroxidase center. The latter Zn2+ is displaced by incoming iron, such that Zn(II)-Fe(III) complexes are formed upon oxidation
additional information
ferritin is a ubiquitous iron storage protein that possesses ferroxidase activity
additional information
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ferritin is a ubiquitous iron storage protein that possesses ferroxidase activity
additional information
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protein localization patterns and metal-enzyme complexes of Candida albicans wild-type and mutant enzymes compared to Saccharomyces cerevisiae enzymes, overview
additional information
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structure of the diiron binding site of ferritin, overview
additional information
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the organism contains a non-heme iron-containing ferritin with dual ferroxidase and DNA-binding activities, that is upregulate under acid stress, overview. By its binding to DNA under acid stress, HP-ferritin is able to protect DNA from oxidative damage caused by free radicals in the presence of metal ions such as iron and copper, overview
additional information
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Dps protein structure and mechanism for ferroxidase-mediated biomineralization, overview
additional information
Dps protein structure and mechanism for ferroxidase-mediated biomineralization, overview. Vibrio cholerae Dps (VcDps) and DpsA representing type I and II channels
additional information
encapsulin A is comprising 180 virus-like structural proteins with an outer diameter of 32 nm. Mechanism for ferroxidase-mediated biomineralization, overview
additional information
encapsulin is comprising 60 virus-like structural proteins with an outer diameter of 24 nm. Mechanism for ferroxidase-mediated biomineralization, overview
additional information
in the dodecameric Dps, translocation position T3 is located at the channel exit where conserved Asp residues narrow the pore diameter significantly, forming a scaffold for tethering ions at the inner wall of the protein. After crossing the constriction zone, three ferroxidase centers are located about 20 A apart and iron can move along negatively charged residues at the inner wall towards the ferroxidase center with high-affinity binding. Mechanism for ferroxidase-mediated biomineralization, overview
additional information
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residue Asp140 and previously identified residues Glu57 andGlu136 are essential residues to promote the iron oxidation at the ferroxidase site, but the presence of these three carboxylate moieties in close proximity to the catalytic centers is not essential to achieve binding of the Fe2+ substrate to the diferric ferroxidase sites with the same coordination geometries as in the wild-type cages
additional information
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residues His25, His37, Asp52, and Glu56 are perfectly conserved among HP-NAPs, dodecameric ferritin, and Dps proteins, and play important roles in metal-ion binding
additional information
the dodecameric Dps protein with an outer particle radius of 8 nm and a storage capacity of about 500 iron atoms. Ferritin can be assembled using six tetramers per cubic face, while Dps complexes are formed through the assembly of six protein dimers on each plane of the cube. Mechanism for ferroxidase-mediated biomineralization, overview
additional information
the recombinant Chlorobium tepidum ferritin (rCtFtn) has an unusual C-terminal region composed of 12 histidine residues, as well as aspartate and glutamate residues. These residues act as potential metal ion ligands, and the rCtFtn homology model predicts that this region projects inside the protein cage. The rCtFtn also lacks a conserved Tyr residue in position 19. The C-terminal region plays an important role in the activity of the ferroxidase center and the stability of rCtFtn. Homology modeling of the subunit of rCtFtn shows that the protein acquires the typical 5 alpha-helix bundle observed for other ferritin subunits
additional information
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the recombinant Chlorobium tepidum ferritin (rCtFtn) has an unusual C-terminal region composed of 12 histidine residues, as well as aspartate and glutamate residues. These residues act as potential metal ion ligands, and the rCtFtn homology model predicts that this region projects inside the protein cage. The rCtFtn also lacks a conserved Tyr residue in position 19. The C-terminal region plays an important role in the activity of the ferroxidase center and the stability of rCtFtn. Homology modeling of the subunit of rCtFtn shows that the protein acquires the typical 5 alpha-helix bundle observed for other ferritin subunits
additional information
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residues His25, His37, Asp52, and Glu56 are perfectly conserved among HP-NAPs, dodecameric ferritin, and Dps proteins, and play important roles in metal-ion binding
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additional information
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Dps protein structure and mechanism for ferroxidase-mediated biomineralization, overview. Vibrio cholerae Dps (VcDps) and DpsA representing type I and II channels
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additional information
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encapsulin A is comprising 180 virus-like structural proteins with an outer diameter of 32 nm. Mechanism for ferroxidase-mediated biomineralization, overview
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additional information
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in the dodecameric Dps, translocation position T3 is located at the channel exit where conserved Asp residues narrow the pore diameter significantly, forming a scaffold for tethering ions at the inner wall of the protein. After crossing the constriction zone, three ferroxidase centers are located about 20 A apart and iron can move along negatively charged residues at the inner wall towards the ferroxidase center with high-affinity binding. Mechanism for ferroxidase-mediated biomineralization, overview
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additional information
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the recombinant Chlorobium tepidum ferritin (rCtFtn) has an unusual C-terminal region composed of 12 histidine residues, as well as aspartate and glutamate residues. These residues act as potential metal ion ligands, and the rCtFtn homology model predicts that this region projects inside the protein cage. The rCtFtn also lacks a conserved Tyr residue in position 19. The C-terminal region plays an important role in the activity of the ferroxidase center and the stability of rCtFtn. Homology modeling of the subunit of rCtFtn shows that the protein acquires the typical 5 alpha-helix bundle observed for other ferritin subunits
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additional information
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the dodecameric Dps protein with an outer particle radius of 8 nm and a storage capacity of about 500 iron atoms. Ferritin can be assembled using six tetramers per cubic face, while Dps complexes are formed through the assembly of six protein dimers on each plane of the cube. Mechanism for ferroxidase-mediated biomineralization, overview
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