1RQ1
Structure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell
Summary for 1RQ1
| Entry DOI | 10.2210/pdb1rq1/pdb |
| Related | 1RP4 |
| Descriptor | Hypothetical 65.0 kDa protein in COX14-COS3 intergenic region precursor, CADMIUM ION, 1-ETHYL-PYRROLIDINE-2,5-DIONE, ... (5 entities in total) |
| Functional Keywords | flavoenzyme, disulfide bonds, cxxcxxc, oxidoreductase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side: Q03103 |
| Total number of polymer chains | 1 |
| Total formula weight | 45589.53 |
| Authors | Gross, E.,Kastner, D.B.,Kaiser, C.A.,Fass, D. (deposition date: 2003-12-04, release date: 2004-06-08, Last modification date: 2024-10-30) |
| Primary citation | Gross, E.,Kastner, D.B.,Kaiser, C.A.,Fass, D. Structure of ero1p, source of disulfide bonds for oxidative protein folding in the cell. Cell(Cambridge,Mass.), 117:601-610, 2004 Cited by PubMed Abstract: The flavoenzyme Ero1p produces disulfide bonds for oxidative protein folding in the endoplasmic reticulum. Disulfides generated de novo within Ero1p are transferred to protein disulfide isomerase and then to substrate proteins by dithiol-disulfide exchange reactions. Despite this key role of Ero1p, little is known about the mechanism by which this enzyme catalyzes thiol oxidation. Here, we present the X-ray crystallographic structure of Ero1p, which reveals the molecular details of the catalytic center, the role of a CXXCXXC motif, and the spatial relationship between functionally significant cysteines and the bound cofactor. Remarkably, the Ero1p active site closely resembles that of the versatile thiol oxidase module of Erv2p, a protein with no sequence homology to Ero1p. 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. PubMed: 15163408DOI: 10.1016/S0092-8674(04)00418-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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