View source for 7cto


==Staphylococcus aureus MsrB==
<StructureSection load='7cto' size='340' side='right'caption='[[7cto]], [[Resolution|resolution]] 3.47&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7cto]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CTO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CTO 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]] 3.47&#8491;</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=7cto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cto OCA], [https://pdbe.org/7cto PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cto RCSB], [https://www.ebi.ac.uk/pdbsum/7cto PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cto ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/W8TTH3_STAAU W8TTH3_STAAU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Oxidative modification of protein structure has been shown to play a significant role in bacterial virulence and metabolism. The sulfur-containing residues are susceptible to oxidation and the enzymatic reversal of oxidized cysteine or methionine is detected in many organisms. Methionine sulfoxide reductases (Msr) are responsible for reducing oxidized methionine. The two different Msrs, MsrA and MsrB, reduce methionine R-sulfoxide and methionine S-sulfoxide, respectively through self-oxidation. This study elucidated the structure of MsrB from Staphylococcus aureus Mu50 and its changes upon oxidation. The active site shows two reduced cysteines in a close contact, implying disulfide bond would form without major structural rearrangement. When the protein is exposed to an oxidative condition, a dimeric state is observed. The dimerization of SAMsrB creates a valley structure for accepting peptidyl substrates. To the best of our knowledge, oxidation induced dimerization of SAMsrB would help to understand mechanism behind redox control that has not been well characterized.

Implication of Staphylococcus aureus MsrB dimerization upon oxidation.,Kim HJ Biochem Biophys Res Commun. 2020 Sep 14. pii: S0006-291X(20)31667-3. doi:, 10.1016/j.bbrc.2020.08.070. PMID:32943184<ref>PMID:32943184</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7cto" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Kim HJ]]