2v1m: Difference between revisions
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<StructureSection load='2v1m' size='340' side='right'caption='[[2v1m]], [[Resolution|resolution]] 1.00Å' scene=''> | <StructureSection load='2v1m' size='340' side='right'caption='[[2v1m]], [[Resolution|resolution]] 1.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2v1m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2v1m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schistosoma_mansoni Schistosoma mansoni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V1M FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=LI:LITHIUM+ION'>LI</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
< | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v1m OCA], [https://pdbe.org/2v1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v1m RCSB], [https://www.ebi.ac.uk/pdbsum/2v1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v1m ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v1m OCA], [https://pdbe.org/2v1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v1m RCSB], [https://www.ebi.ac.uk/pdbsum/2v1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v1m ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/GPX1_SCHMA GPX1_SCHMA] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Angelucci | [[Category: Schistosoma mansoni]] | ||
[[Category: Bellelli | [[Category: Angelucci F]] | ||
[[Category: Boumis | [[Category: Bellelli A]] | ||
[[Category: Brunori | [[Category: Boumis G]] | ||
[[Category: Dimastrogiovanni | [[Category: Brunori M]] | ||
[[Category: Miele | [[Category: Dimastrogiovanni D]] | ||
[[Category: Miele AE]] | |||
Latest revision as of 18:02, 13 December 2023
Crystal structure of Schistosoma mansoni glutathione peroxidaseCrystal structure of Schistosoma mansoni glutathione peroxidase
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedOxidative 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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