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Article

A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p.

Nature structural biology - 1 Jan 2002

Gross Einav, Sevier Carolyn S, Vala Andrea, Kaiser Chris A, Fass Deborah

Abstract excerpt

Erv2p is an FAD-dependent sulfhydryl oxidase that can promote disulfide bond formation during protein biosynthesis in the yeast endoplasmic reticulum. The structure of Erv2p, determined by X-ray crystallography to 1.5 A resolution, reveals a helix-rich dimer with no global resemblance to other known FAD-binding proteins or thiol oxidoreductases. Two pairs of cysteine residues are required for Erv2p activity. The...

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PMID: 11740506
DOI: 10.1038/nsb740

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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