1JRA
Crystal Structure of Erv2p
Summary for 1JRA
| Entry DOI | 10.2210/pdb1jra/pdb |
| Related | 1JR8 |
| Descriptor | ERV2 PROTEIN, MITOCHONDRIAL, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | fad, sulfhydryl oxidase, helical bundle, cxxc, oxidoreductase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Endoplasmic reticulum membrane; Single-pass type III membrane protein; Lumenal side: Q12284 |
| Total number of polymer chains | 4 |
| Total formula weight | 57239.62 |
| Authors | Gross, E.,Sevier, C.S.,Vala, A.,Kaiser, C.A.,Fass, D. (deposition date: 2001-08-13, release date: 2001-12-28, Last modification date: 2024-11-13) |
| Primary citation | Gross, E.,Sevier, C.S.,Vala, A.,Kaiser, C.A.,Fass, D. A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nat.Struct.Biol., 9:61-67, 2002 Cited by PubMed Abstract: 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 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. PubMed: 11740506DOI: 10.1038/nsb740 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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