Cloned (Comment) | Organism |
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- |
Saccharomyces cerevisiae |
Crystallization (Comment) | Organism |
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crystal structures at 2.0 A resolution of the C-terminal domain and at 3.0 A resolution of a C30S/C133S double mutant. The C-terminal domain exists as a homodimer, with each subunit consisting of a conserved four-helix bundle that accommodates the isoalloxazine ring of FAD and an additional single-turn helix. The N-terminal domain is an amphipathic helix flanked by two flexible loops. This structure also represents an intermediate state of electron transfer from the N-terminal domain to the C-terminal domain of another subunit. The four-helix bundle of the C-terminal domain forms a wide platform for the electron donor N-terminal domain. Moreover,the amphipathic helix close to the shuttle redox enter may be critical for the recognition of Mia40, the upstream electron donor | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
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Organism | UniProt | Comment | Textmining |
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Saccharomyces cerevisiae | P27882 | - |
- |
Synonyms | Comment | Organism |
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Erv1 | - |
Saccharomyces cerevisiae |
mitochondrial FAD-linked sulfhydryl oxidase ERV1 | - |
Saccharomyces cerevisiae |