High impact information on ERV2

• Remarkably, the Ero1p active site closely resembles that of the versatile thiol oxidase module of Erv2p, a protein with no sequence homology to Ero1p [1].
• ERV2 encodes a luminal ER protein of relative molecular mass 22,000 [2].
• Purified recombinant Erv2p is a flavoenzyme that can catalyse O2-dependent formation of disulphide bonds [2].
• A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p [3].
• Two pairs of cysteine residues are required for Erv2p activity [3].

Biological context of ERV2

• Furthermore, both Ero1p and Erv2p display essential dicysteine motifs on mobile polypeptide segments, suggesting that shuttling electrons to a rigid active site using a flexible strand is a fundamental feature of disulfide-generating flavoenzymes [1].
• Erv2p is an FAD-dependent sulfhydryl oxidase that can promote disulfide bond formation during protein biosynthesis in the yeast endoplasmic reticulum [3].
• These mutants were found to disrupt Erv2p dimerization and to increase the activity of Erv2p for thiol substrates such as glutathione [4].

Associations of ERV2 with chemical compounds

• Further characterization of the fragments and insights gained from the crystal structure of yeast ERV2p (Gross, E., Sevier, C. S., Vala, A., Kaiser, C. A., and Fass, D. (2002) Nat. Struct. Biol. 9, 61-67) suggest that the flow of reducing equivalents in intact avian QSOX is dithiol substrate --> C80/83 --> C519/522 --> C459/462 --> FAD --> oxygen [5].

Analytical, diagnostic and therapeutic context of ERV2

• 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 [3].

References