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Literature summary for 1.8.3.2 extracted from

  • Guo, P.C.; Ma, J.D.; Jiang, Y.L.; Wang, S.J.; Bao, Z.Z.; Yu, X.J.; Chen, Y.; Zhou, C.Z.
    Structure of yeast sulfhydryl oxidase erv1 reveals electron transfer of the disulfide relay system in the mitochondrial intermembrane space (2012), J. Biol. Chem., 287, 34961-34969.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P27882
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Synonyms

Synonyms Comment Organism
Erv1
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Saccharomyces cerevisiae
mitochondrial FAD-linked sulfhydryl oxidase ERV1
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Saccharomyces cerevisiae