4mn7

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==Structural and biochemical analysis of type II free methionine-R-sulfoxide reductase from Thermoplasma acidophilum==
==Structural and biochemical analysis of type II free methionine-R-sulfoxide reductase from Thermoplasma acidophilum==
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<StructureSection load='4mn7' size='340' side='right' caption='[[4mn7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='4mn7' size='340' side='right'caption='[[4mn7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4mn7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MN7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MN7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4mn7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum_DSM_1728 Thermoplasma acidophilum DSM 1728]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MN7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MN7 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SME:METHIONINE+SULFOXIDE'>SME</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mmn|4mmn]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SME:METHIONINE+SULFOXIDE'>SME</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mn7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mn7 RCSB], [http://www.ebi.ac.uk/pdbsum/4mn7 PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4mn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mn7 OCA], [https://pdbe.org/4mn7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mn7 RCSB], [https://www.ebi.ac.uk/pdbsum/4mn7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mn7 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9HJW5_THEAC Q9HJW5_THEAC]
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Free methionine-R-sulfoxide reductase (fRMsr) enzymes only reduce the free form of methionine-R-sulfoxide and can be grouped into two types with respect to the number of conserved Cys residues in the active sites. In this work, the crystal structures of type II fRMsr from Thermoplasma acidophilum (TafRMsr), which contains two conserved Cys, have been determined in native form and in a complex with the substrate. The overall structure of TafRMsr consists of a central beta-sheet encompassed by a two-alpha-helix bundle flanking on one side and one small alpha-helix on the other side. Based on biochemical and growth complementation assays, Cys84 is demonstrated to be the catalytic Cys. The data also show that TafRMsr functions as an antioxidant protein. Structural analyses reveal insights into substrate recognition and orientation, conformational changes in the active site during substrate binding, and the role of active site residues in substrate binding. A model for the catalytic mechanism of type II TafRMsr is suggested, in which intramolecular disulfide bond formation is not involved. In addition, the biochemical, enzymatic, and structural properties of type II TafRMsr are compared with those of type I enzymes.
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Structural and biochemical analysis of a type II free methionine-R-sulfoxide reductase from Thermoplasma acidophilum.,Kim HS, Kwak GH, Lee K, Jo CH, Hwang KY, Kim HY Arch Biochem Biophys. 2014 Jul 17. pii: S0003-9861(14)00252-5. doi:, 10.1016/j.abb.2014.07.009. PMID:25043974<ref>PMID:25043974</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Hwang, K Y]]
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[[Category: Large Structures]]
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[[Category: Jo, C H]]
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[[Category: Thermoplasma acidophilum DSM 1728]]
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[[Category: Kim, H S]]
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[[Category: Hwang KY]]
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[[Category: Kim, H Y]]
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[[Category: Jo CH]]
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[[Category: Kwak, G H]]
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[[Category: Kim HS]]
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[[Category: Lee, K T]]
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[[Category: Kim HY]]
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[[Category: Oxidoreductase]]
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[[Category: Kwak GH]]
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[[Category: Reductase]]
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[[Category: Lee KT]]

Current revision

Structural and biochemical analysis of type II free methionine-R-sulfoxide reductase from Thermoplasma acidophilum

PDB ID 4mn7

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