x * 28085, a 26-residue signal peptide is cleaved off by the Escherichia coli processing machinery, thus the recombinant enzyme has a MW of 26314 Da, calculation from nucleotide sequence
most alphaCA enzymes are monomeric, but alphaCA1 from Chlamydomonas reinhardtii is a dimer that is uniquely stabilized by disulfide bonds, crystal structure determination and analysis
enzyme CrCAH3 is a dimer at pH 4.1 that is stabilized by swapping of the N-terminal arms, a feature not previously observed in alpha-type carbonic anhydrases
enzyme Cab is a dimer with the typical alpha/beta fold of beta-CAs. The two monomers within the dimer are related by a 2fold axis and their structure consists of a central beta-sheet core composed of five strands. Upon dimer formation, an extended beta-sheet core encompassing the entire dimer is formed. Several alpha-helices pack onto this beta-structural motif, resulting in a large interface area between the two enzyme subunits
enzyme Cab is a dimer with the typical alpha/beta fold of beta-CAs. The two monomers within the dimer are related by a 2fold axis and their structure consists of a central beta-sheet core composed of five strands. Upon dimer formation, an extended beta-sheet core encompassing the entire dimer is formed. Several alpha-helices pack onto this beta-structural motif, resulting in a large interface area between the two enzyme subunits
enzyme CcaA shows a wellpacked trimer-of-dimers organization. The proximal part of the characteristic C-terminal extension is ordered by binding at a site that passes through the two-fold symmetry axis shared with an adjacent dimer, as a result, only one of a pair of converging termini can be ordered at any given time. beta-CA structures are organized around a tight, catalytic dimer. The catalytic site of CcaA is located at the interface between two protomers, with the zinc ion bound to Cys39, His98, and Cys101. A water molecule forms the fourth zinc ligand at pH 4.5
SazCA enzyme three-dimensional structure determination and analysis, structure comparison with the enzyme from Sulfurihydrogenibium yellowstonensis, PDB ID 4G7A. The SazCA monomer adopts the canonical fold of the alpha-CA family members consisting of a central ten-stranded beta-sheet surrounded by alpha- and 310-helices as well as small additional beta-sheets. The active site of each monomer within the dimer is completely accessible to the solvent and, as observed for other alpha-CAs, is located in a cavity which extends from the surface to the center of the protein
SazCA enzyme three-dimensional structure determination and analysis, structure comparison with the enzyme from Sulfurihydrogenibium yellowstonensis, PDB ID 4G7A. The SazCA monomer adopts the canonical fold of the alpha-CA family members consisting of a central ten-stranded beta-sheet surrounded by alpha- and 310-helices as well as small additional beta-sheets. The active site of each monomer within the dimer is completely accessible to the solvent and, as observed for other alpha-CAs, is located in a cavity which extends from the surface to the center of the protein
x * 27000 + x * 27500, chloroplastic isoenzyme, the two subunits are identical, except that the 27000 Da subunit is three amino acids shorter than the 27500 Da subunit, SDS-PAGE
recombinant Co-HICA, the crystal structure shows a four-coordinate geometry for Co-HICA with pH-dependent changes in the absorption spectrum of Co-HICA, overview
cross-sectional profiles of the gamma-CA trimer reveal that each monomer resembles an equilateral triangle, which is stabilized by hydrogen bonds, salt bridges and hydrophobic interactions. The trimer contains 3 active sites and each monomer contributes His residues located on the surface to coordinate the Zn(II) ion crucial for catalysis
cross-sectional profiles of the gamma-CA trimer reveal that each monomer resembles an equilateral triangle, which is stabilized by hydrogen bonds, salt bridges and hydrophobic interactions. The trimer contains 3 active sites and each monomer contributes His residues located on the surface to coordinate the Zn(II) ion crucial for catalysis
cross-sectional profiles of the gamma-CA trimer reveal that each monomer resembles an equilateral triangle, which is stabilized by hydrogen bonds, salt bridges and hydrophobic interactions. The trimer contains 3 active sites and each monomer contributes His residues located on the surface to coordinate the Zn(II) ion crucial for catalysis
overall secondary and tertiary structure of Co-HICA differ from wild-type Zn-enzyme structure, active R-state and inactive T-state conformations, overview
the studied anion binding site along the dimerization interface of HICA is an escort site that represents an intermediate along the ingress/egress route of bicarbonate ion to/from the allosteric binding site, overview. Type II beta-CAs can also adopt an active, R-state conformation in which Asp44 pairs with Arg46, allowing the coordination of the catalytically essential water molecule to the active site zinc ion. The noncatalytic bicarbonate ion stabilizes the inactive T state
the studied anion binding site along the dimerization interface of HICA is an escort site that represents an intermediate along the ingress/egress route of bicarbonate ion to/from the allosteric binding site, overview. Type II beta-CAs can also adopt an active, R-state conformation in which Asp44 pairs with Arg46, allowing the coordination of the catalytically essential water molecule to the active site zinc ion. The noncatalytic bicarbonate ion stabilizes the inactive T state
the active form of CAIX in the MDA-MB-231 breast cancer cell line is dimeric but that neither lipid raft localization nor phosphorylation are likely required for its dimerization or activity
CA XIV is a membrane-associated glycoprotein composed of an extracellular catalytic domain, a single transmembrane helix, and a short intracellular polypeptide chain. The protein has two cysteine residues that form a disulfide bond for the stabilization of CA XIV structure and one N-glycosylation site
CA XIV is a membrane-associated glycoprotein composed of an extracellular catalytic domain, a single transmembrane helix, and a short intracellular polypeptide chain. The protein has two cysteine residues that form a disulfide bond for the stabilization of CA XIV structure and one N-glycosylation site
isozyme HCAII is a beta-sheet dominated monomeric protein of 259 aminoacid residues. The far-UV CD is used to characterize the intermediate states (XI and XII) for secondary structural content, near-UV CD for tertiary structure, dynamic light scatteringfor hydrodynamic radius and ANS fluorescence spectroscopy for the presence of exposed hydrophobic patches. Stable intermediates XI and XII populations of intermediates are prepared by urea-derived protein denaturation at around 2 and 4 M urea, respectively. Urea-induced XI state has characteristics ofmolten globule state while XII state bears characteristics features of pre-molten globule state, overview
isozyme HCAII is a beta-sheet dominated monomeric protein of 259 aminoacid residues. The far-UV CD is used to characterize the intermediate states (XI and XII) for secondary structural content, near-UV CD for tertiary structure, dynamic light scatteringfor hydrodynamic radius and ANS fluorescence spectroscopy for the presence of exposed hydrophobic patches. Stable intermediates XI and XII populations of intermediates are prepared by urea-derived protein denaturation at around 2 and 4 M urea, respectively. Urea-induced XI state has characteristics ofmolten globule state while XII state bears characteristics features of pre-molten globule state, overview
peptide mass finger prints by tryptic digestion and mass spectrometry. Secondary structure of enzyme CAVA is measured using circular dichroism. The secondary structural contents for the native CAVA include 20.2% alpha-helix, 29.1% beta-sheet and 50.7% random coil, while the renatured CAVA has 21.7% alpha-helix, 27.2% beta-sheet, and 51.3% random coil, and the denatured CAVA has 15.3% alpha-helix, 21.7% beta-sheet, and 63% random coil
peptide mass finger prints by tryptic digestion and mass spectrometry. Secondary structure of enzyme CAVA is measured using circular dichroism. The secondary structural contents for the native CAVA include 20.2% alpha-helix, 29.1% beta-sheet and 50.7% random coil, while the renatured CAVA has 21.7% alpha-helix, 27.2% beta-sheet, and 51.3% random coil, and the denatured CAVA has 15.3% alpha-helix, 21.7% beta-sheet, and 63% random coil
the extracellular region of the isozyme consists of the catalytic CA domain and the proteoglycan-like (PG) domain, PG domain structure determination and analysis, overview. The isolated PG domain belongs to the family of intrinsically disordered proteins, being globally unfolded with only some local residual polyproline II secondary structure, it shows conformational flexibility. Primary sequence analysis of the PG(38-136) protein, peptide analysis by gel filtration, NMR spectroscopy, and dynamic light scattering, modelling and molecular dynamics studies, overview
the extracellular region of the isozyme consists of the catalytic CA domain and the proteoglycan-like (PG) domain, PG domain structure determination and analysis, overview. The isolated PG domain belongs to the family of intrinsically disordered proteins, being globally unfolded with only some local residual polyproline II secondary structure, it shows conformational flexibility. Primary sequence analysis of the PG(38-136) protein, peptide analysis by gel filtration, NMR spectroscopy, and dynamic light scattering, modelling and molecular dynamics studies, overview
the dimeric enzyme TcruCA has a highly conserved yet compact structure compared with other alpha-CAs, interface structure, structure comparisons, detailed overview. The TcruCA monomer has the signature secondary structure typical of an alpha-CA fold, with helical and loop structures present towards the surface and a conical active-site cavity comprised of mostly beta-structure
the dimeric enzyme TcruCA has a highly conserved yet compact structure compared with other alpha-CAs, interface structure, structure comparisons, detailed overview. The TcruCA monomer has the signature secondary structure typical of an alpha-CA fold, with helical and loop structures present towards the surface and a conical active-site cavity comprised of mostly beta-structure
enzyme Cab shows significant structural differences with respect to the other enzymes of beta-class in the N-terminus, C-terminus and in the region encompassing residues 90-125. Moreover, it presents a less extended C-terminal region, being the smallest beta-CA so far characterized
enzyme Cab shows significant structural differences with respect to the other enzymes of beta-class in the N-terminus, C-terminus and in the region encompassing residues 90-125. Moreover, it presents a less extended C-terminal region, being the smallest beta-CA so far characterized
the alpha-CA presents a fold characterized by a central ten-stranded beta-sheet surrounded by several helices and additional beta-strands. The active site is found in a deep conical cavity which extends from the protein surface to the center of the molecule, with the catalytic zinc ion positioned at the bottom of this cavity
CcmM is built as two distinct regions, the C-terminal region of CcmM consists of three to five repeats of a RubisCO small subunit-like domain, separated by flexible linker regions. This region binds RubisCO. The N-terminal domain is clearly homologous to gamma-CAs, but in at least some strains, including Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7942, this domain lacks measurable CA activity. CcmM's N-terminal domain is trimeric. The C-terminal end of the eta-helix is dominated by the protruding alphaA helix and the alphaA-alphaB loop