Cloned (Comment) | Organism |
---|---|
recombinant coexpression of Pex1 and Pex6 in yeast cells with an N-terminal SBP tag on Pex1 and an N-terminal His14 tag on Pex6 | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
peroxisome | peroxisomal Pex1/Pex6 ATPase complex | Saccharomyces cerevisiae | 5777 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | Saccharomyces cerevisiae | - |
ADP + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P24004 | PEX1 | - |
Saccharomyces cerevisiae | P33760 | PEX6 | - |
Purification (Comment) | Organism |
---|---|
co-purification of recombinant Strep-tagged Pex1 and His6-tagged Pex6 from yeast cells by sequential affinity chromatography on Ni-NTA and streptavidin agarose resins, followed by gel filtration | Saccharomyces cerevisiae |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + H2O = ADP + phosphate | ATP hydrolysis occurs in a unidirectional manner around the ring, with one subunit primarily affecting ATP hydrolysis of only one of the neighboring subunits. ATP binding is initiated on one side of the ring at the nucleotide-free sites where the subunits are most widely spaced | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | - |
Saccharomyces cerevisiae | ADP + phosphate | - |
? | |
ATP + H2O | nucleotide hydrolysis by the ATPase domain of Pex1 | Saccharomyces cerevisiae | ADP + phosphate | - |
? | |
ATP + H2O | nucleotide hydrolysis by the ATPase domain of Pex6 | Saccharomyces cerevisiae | ADP + phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterohexamer | the enzyme complex exhibts a unique double-ring structure, cryo-electron microscopy | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
peroxisomal Pex1/Pex6 ATPase complex | - |
Saccharomyces cerevisiae |
Pex1 | - |
Saccharomyces cerevisiae |
Pex1/Pex6 complex | - |
Saccharomyces cerevisiae |
PEX6 | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
evolution | Pex1 and Pex6 are members of the AAA family of ATPases | Saccharomyces cerevisiae |
malfunction | mutations in the proteins frequently cause peroxisomal diseases | Saccharomyces cerevisiae |
additional information | enzyme Pex1p/Pex6p complex structure modeling using a computational approach that combines Monte Carlo placement of structurally homologous domains into density maps with energy minimization and refinement protocols. Pex1 and Pex6 assemble into hexameric double rings and perform vital functions, structure-function relationship, molecular models. Comparison of the structures of the Pex1/Pex6 complex determined in presence of ATPgammaS and ADP | Saccharomyces cerevisiae |
physiological function | ATP hydrolysis at both Pex1p/Pex6p complex sites is needed for cell viability | Saccharomyces cerevisiae |