1rp4 | pdb_00001rp4

Structure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell

spinqualitylabelsall models 1rp4, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1rp4 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: CD, FAD, MSE, NEN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ERO1_YEAST Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly PDI1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on PDI1 to transfer oxidizing equivalent. Also able to oxidize directly the PDI related protein MPD2. Does not oxidize all PDI related proteins, suggesting that it can discriminate between PDI1 and related proteins. Reoxidation of ERO1 probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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