4f9z | pdb_00004f9z

Crystal Structure of human ERp27

spinqualitylabelsall models 4f9z, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4f9z is a 5 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, PE3, PE4 Related: 2l4c Gene: C12orf46, ERP27, UNQ781/PRO1575 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed About one-third of all cellular proteins pass through the secretory pathway and hence undergo oxidative folding in the endoplasmic reticulum (ER). Protein-disulfide isomerase (PDI) and related members of the PDI family assist in the folding of substrates by catalyzing the oxidation of two cysteines and isomerization of disulfide bonds as well as by acting as chaperones. In this study, we present the crystal structure of ERp27, a redox-inactive member of the PDI family. The structure reveals its substrate-binding cleft, which is homologous to PDI, but is able to adapt in size and hydrophobicity. Isothermal titration calorimetry experiments demonstrate that ERp27 is able to distinguish between folded and unfolded substrates, only interacting with the latter. ERp27 is up-regulated during ER stress, thus presumably allowing it to bind accumulating misfolded substrates and present them to ERp57 for catalysis. The Crystal Structure of the Protein-Disulfide Isomerase Family Member ERp27 Provides Insights into Its Substrate Binding Capabilities.,Kober FX, Koelmel W, Kuper J, Drechsler J, Mais C, Hermanns HM, Schindelin H J Biol Chem. 2013 Jan 18;288(3):2029-39. doi: 10.1074/jbc.M112.410522. Epub 2012 , Nov 28. PMID:23192347 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ER-resident protein

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