View source for 4lwj


==Crystal structure of methionine sulfoxide reductase U16C from clostridium oremlandii==
<StructureSection load='4lwj' size='340' side='right'caption='[[4lwj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4lwj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkaliphilus_oremlandii_OhILAs Alkaliphilus oremlandii OhILAs]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LWJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<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=CSO:S-HYDROXYCYSTEINE'>CSO</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=4lwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lwj OCA], [https://pdbe.org/4lwj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lwj RCSB], [https://www.ebi.ac.uk/pdbsum/4lwj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lwj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A8MI53_ALKOO 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]
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== 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<ref>PMID:24412203</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4lwj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Alkaliphilus oremlandii OhILAs]]
[[Category: Large Structures]]
[[Category: Hwang KY]]
[[Category: Lee EH]]