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| | ==Induced Dimer Structure of Methionine Sulfoxide Reductase U16C from Clostridium Oremlandii== | | ==Induced Dimer Structure of Methionine Sulfoxide Reductase U16C from Clostridium Oremlandii== |
| - | <StructureSection load='4u66' size='340' side='right' caption='[[4u66]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='4u66' size='340' side='right'caption='[[4u66]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4u66]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U66 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4u66]] is a 3 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=4U66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U66 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide-methionine_(S)-S-oxide_reductase Peptide-methionine (S)-S-oxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.11 1.8.4.11] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4u66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u66 OCA], [http://pdbe.org/4u66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u66 RCSB], [http://www.ebi.ac.uk/pdbsum/4u66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u66 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=4u66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u66 OCA], [https://pdbe.org/4u66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u66 RCSB], [https://www.ebi.ac.uk/pdbsum/4u66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u66 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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] | + | [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] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hwang, K Y]] | + | [[Category: Alkaliphilus oremlandii OhILAs]] |
| - | [[Category: Lee, E H]] | + | [[Category: Large Structures]] |
| - | [[Category: Alpha/beta fold]] | + | [[Category: Hwang KY]] |
| - | [[Category: Oxidoreductase]] | + | [[Category: Lee EH]] |
| Structural highlights
Function
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]
Publication Abstract from PubMed
Clostridium oremlandii MsrA (CoMsrA) is a natively selenocysteine-containing methionine-S-sulfoxide reductase and classified into a 1-Cys type MsrA. CoMsrA exists as a monomer in solution. Herein, we report evidence that CoMsrA can undergo homodimerization during catalysis. The monomeric CoMsrA dimerizes in the presence of its substrate methionine sulfoxide via an intermolecular disulfide bond between catalytic Cys16 residues. The dimeric CoMsrA is resolved by the reductant glutaredoxin, suggesting the relevance of dimerization in catalysis. The dimerization reaction occurs in a concentration- and time-dependent manner. In addition, the occurrence of homodimer formation in the native selenoprotein CoMsrA is confirmed. We also determine the crystal structure of the dimeric CoMsrA, having the dimer interface around the two catalytic Cys16 residues. A central cone-shaped hole is present in the surface model of dimeric structure, and the two Cys16 residues constitute the base of the hole. Collectively, our biochemical and structural analyses suggest a novel dimerization-mediated mechanism for CoMsrA catalysis that is additionally involved in CoMsrA regeneration by glutaredoxin.
Evidence for the Dimerization-Mediated Catalysis of Methionine Sulfoxide Reductase A from Clostridium oremlandii.,Lee EH, Lee K, Kwak GH, Park YS, Lee KJ, Hwang KY, Kim HY PLoS One. 2015 Jun 24;10(6):e0131523. doi: 10.1371/journal.pone.0131523., eCollection 2015. PMID:26107511[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lee EH, Lee K, Kwak GH, Park YS, Lee KJ, Hwang KY, Kim HY. Evidence for the Dimerization-Mediated Catalysis of Methionine Sulfoxide Reductase A from Clostridium oremlandii. PLoS One. 2015 Jun 24;10(6):e0131523. doi: 10.1371/journal.pone.0131523., eCollection 2015. PMID:26107511 doi:http://dx.doi.org/10.1371/journal.pone.0131523
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