Protein Variants | Comment | Organism |
---|---|---|
K30C/A276C | alpha3beta3gamma, the mutant shows assembly as the wild-type enzyme complex | Rhodospirillum rubrum |
K30C/R278C | alpha3beta3gamma, the mutant shows assembly as the wild-type enzyme complex | Rhodospirillum rubrum |
additional information | pairs of cysteine residues were introduced into the twisted N- and C-terminal helices of the gamma subunit of the chloroplast F1-ATPase to test, via disulfide cross-linking, potential inter-helical movements involved in catalysis of ATP hydrolysis. Significant disulfide formation of 50-75% is observed between cysteines introduced at positions 30 and 31 in the N-terminal helix and 276 and 278 in the C-terminal helix, cross-linking has no apparent effect on catalysis | Rhodospirillum rubrum |
V31C/A276C | alpha3beta3gamma, the mutant shows assembly as the wild-type enzyme complex | Rhodospirillum rubrum |
V31C/R278C | alpha3beta3gamma, the mutant shows assembly as the wild-type enzyme complex | Rhodospirillum rubrum |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
chloroplast | - |
Rhodospirillum rubrum | 9507 | - |
membrane | - |
Rhodospirillum rubrum | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodospirillum rubrum | - |
- |
- |
Subunits | Comment | Organism |
---|---|---|
multimer | the ATP synthase enzymes of chloroplasts is composed of two protein segments, FO and F1, the chloroplast FO1 contains four different polypeptide subunits with a stoichiometry of I1II1III14IV1. The F1 segment contains the catalytic sites for ATP synthesis and hydrolysis. The chloroplast F1 is comprised of five different polypeptide subunits, alpha to epsilon, with a stoichiometry of alpha3beta3gamma1delta1epsilon1 | Rhodospirillum rubrum |
Synonyms | Comment | Organism |
---|---|---|
photosynthetic F1-ATPase | - |
Rhodospirillum rubrum |