2k8v

Solution structure of Oxidised ERp18

spinqualitylabelsall models 2k8v, 40 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2k8v is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: TXNDC12, TLP19, UNQ713/PRO1376 (HUMAN) Activity: Protein-disulfide reductase (glutathione), with EC number 1.8.4.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TXD12_HUMAN] Possesses significant protein thiol-disulfide oxidase activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Here we report the solution structure of oxidized ERp18 as determined using NMR spectroscopy. ERp18 is the smallest member of the protein disulfide isomerase (PDI) family of proteins to contain a Cys-Xxx-Xxx-Cys active site motif. It is an 18 kDa endoplasmic reticulum resident protein with unknown function although sequence similarity to individual domains of the thiol-disulfide oxidoreductase PDI suggests ERp18 may have a similar structure and function. Like the catalytic domains of PDI, ERp18 adopts a thioredoxin fold with a thioredoxin-like active site located at the N-terminus of a long kinked helix that spans the length of the protein. Comparison of backbone chemical shifts for oxidized and reduced ERp18 shows the majority of residues possess the same backbone conformation in both states, with differences limited to the active site and regions in close proximity. S(2) order parameters from NMR backbone dynamics were found to be 0.81 for oxidized and 0.91 for reduced ERp18, and these observations, in combination with amide hydrogen exchange rates, imply a more rigid and compact backbone for the reduced structure. These observations support a putative role for ERp18 within the cell as an oxidase, introducing disulfide bonds to substrate proteins, providing structural confirmation of ERp18's role as a thiol-disulfide oxidoreductase. Solution Structure and Dynamics of ERp18, a Small Endoplasmic Reticulum Resident Oxidoreductase .,Rowe ML, Ruddock LW, Kelly G, Schmidt JM, Williamson RA, Howard MJ Biochemistry. 2009 May 7. PMID:19361226 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ER-resident protein

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