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| | <StructureSection load='4lwm' size='340' side='right'caption='[[4lwm]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='4lwm' size='340' side='right'caption='[[4lwm]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4lwm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Alkoo Alkoo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LWM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LWM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4lwm]] 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=4LWM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LWM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MHO:S-OXYMETHIONINE'>MHO</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]] 1.804Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lwj|4lwj]], [[4lwk|4lwk]], [[4lwl|4lwl]], [[4lwn|4lwn]]</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=MHO:S-OXYMETHIONINE'>MHO</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">msrA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=350688 ALKOO])</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=4lwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lwm OCA], [https://pdbe.org/4lwm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lwm RCSB], [https://www.ebi.ac.uk/pdbsum/4lwm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lwm ProSAT]</span></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>
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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=4lwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lwm OCA], [http://pdbe.org/4lwm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lwm RCSB], [http://www.ebi.ac.uk/pdbsum/4lwm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lwm 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: Alkoo]] | + | [[Category: Alkaliphilus oremlandii OhILAs]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hwang, K Y]] | + | [[Category: Hwang KY]] |
| - | [[Category: Lee, E H]] | + | [[Category: Lee EH]] |
| - | [[Category: Alpha/beta fold]]
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| - | [[Category: Oxidoreductase]]
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| 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
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lee EH, Kwak GH, Kim MJ, Kim HY, Hwang KY. Structural analysis of 1-Cys type selenoprotein methionine sulfoxide reductase A. Arch Biochem Biophys. 2014 Mar 1;545:1-8. doi: 10.1016/j.abb.2013.12.024. Epub, 2014 Jan 8. PMID:24412203 doi:http://dx.doi.org/10.1016/j.abb.2013.12.024
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