4lwm

Crystal structure of methionine sulfoxide reductase U16C/E55D from clostridium oremlandii with methionie sulfoxide

spinqualitylabelsall models 4lwm, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4lwm is a 1 chain structure with sequence from Alkaliphilus oremlandii OhILAs. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.804Å Ligands: ACT, MHO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A8MI53_ALKOO Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).[HAMAP-Rule:MF_01401] Publication Abstract from PubMed Methionine sulfoxide reductase A (MsrA) reduces free and protein-based methionine-S-sulfoxide to methionine. Structures of 1-Cys MsrAs lacking a resolving Cys, which interacts with catalytic Cys, are unknown. In addition, no structural information on selenocysteine (Sec)-containing MsrA enzymes has been reported. In this work, we determined the crystal structures of 1-Cys type selenoprotein MsrA from Clostridium oremlandii at 1.6-1.8A, including the reduced, oxidized (sulfenic acid), and substrate-bound forms. The overall structure of Clostridium MsrA, consisting of ten alpha-helices and six beta-strands, folds into a catalytic domain and a novel helical domain absent from other known MsrA structures. The helical domain, containing five helices, tightly interacts with the catalytic domain, and is likely critical for catalytic activity due to its association with organizing the active site. This helical domain is also conserved in several selenoprotein MsrAs. Our structural analysis reveals that the side chain length of Glu55 is critical for the proton donor function of this residue. Our structures also provide insights into the architecture of the 1-Cys MsrA active site and the roles of active site residues in substrate recognition and catalysis. Structural analysis of 1-Cys type selenoprotein methionine sulfoxide reductase A.,Lee EH, Kwak GH, Kim MJ, Kim HY, Hwang KY Arch Biochem Biophys. 2014 Mar 1;545:1-8. doi: 10.1016/j.abb.2013.12.024. Epub, 2014 Jan 8. PMID:24412203 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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