1jr8
From Proteopedia
Crystal Structure of Erv2p
Structural highlights
FunctionERV2_YEAST FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation in the endoplasmic reticulum lumen in parallel to ERO1.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedErv2p 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 first (Cys-Gly-Glu-Cys) is adjacent to the isoalloxazine ring of the FAD. The second (Cys-Gly-Cys) is part of a flexible C-terminal segment that can swing into the vicinity of the first cysteine pair in the opposite subunit of the dimer and may shuttle electrons between substrate protein dithiols and the FAD-proximal disulfide. A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p.,Gross E, Sevier CS, Vala A, Kaiser CA, Fass D Nat Struct Biol. 2002 Jan;9(1):61-7. PMID:11740506[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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