2v1m | pdb_00002v1m

Crystal structure of Schistosoma mansoni glutathione peroxidase

spinqualitylabelsall models 2v1m, resolution 1.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2v1m is a 1 chain structure with sequence from Schistosoma mansoni. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1Å Ligands: ACT, LI, OCS, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GPX1_SCHMA 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 Oxidative stress is a widespread challenge for living organisms, and especially so for parasitic ones, given the fact that their hosts can produce reactive oxygen species (ROS) as a mechanism of defense. Thus, long lived parasites, such as the flatworm Schistosomes, have evolved refined enzymatic systems capable of detoxifying ROS. Among these, glutathione peroxidases (Gpx) are a family of sulfur or selenium-dependent isozymes sharing the ability to reduce peroxides using the reducing equivalents provided by glutathione or possibly small proteins such as thioredoxin. As for other frontline antioxidant enzymatic systems, Gpxs are localized in the tegument of the Schistosomes, the outermost defense layer. In this article, we present the first crystal structure at 1.0 and 1.7 A resolution of two recombinant SmGpxs, carrying the active site mutations Sec43Cys and Sec43Ser, respectively. The structures confirm that this enzyme belongs to the monomeric class 4 (phospholipid hydroperoxide) Gpx. In the case of the Sec to Cys mutant, the catalytic Cys residue is oxidized to sulfonic acid. By combining static crystallography with molecular dynamics simulations, we obtained insight into the substrate binding sites and the conformational changes relevant to catalysis, proposing a role for the unusual reactivity of the catalytic residue. Proteins 2009. (c) 2009 Wiley-Liss, Inc. Combining crystallography and molecular dynamics: The case of Schistosoma mansoni phospholipid glutathione peroxidase.,Dimastrogiovanni D, Anselmi M, Miele AE, Boumis G, Petersson L, Angelucci F, Nola AD, Brunori M, Bellelli A Proteins. 2009 Jul 20. PMID:19714775 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glutathione peroxidase

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