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| | <StructureSection load='4w8c' size='340' side='right'caption='[[4w8c]], [[Resolution|resolution]] 1.76Å' scene=''> | | <StructureSection load='4w8c' size='340' side='right'caption='[[4w8c]], [[Resolution|resolution]] 1.76Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4w8c]] is a 2 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=4W8C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4W8C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4w8c]] is a 2 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=4W8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4W8C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</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]] 1.7568Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lwj|4lwj]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">msrA, Clos_1947 ([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=4w8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w8c OCA], [https://pdbe.org/4w8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4w8c RCSB], [https://www.ebi.ac.uk/pdbsum/4w8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4w8c 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=4w8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w8c OCA], [http://pdbe.org/4w8c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4w8c RCSB], [http://www.ebi.ac.uk/pdbsum/4w8c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4w8c 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: Kim, H Y]] | + | [[Category: Kim H-Y]] |
| - | [[Category: Lee, E H]] | + | [[Category: Lee EH]] |
| - | [[Category: Clostridium oremlandii]]
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| - | [[Category: Msra]]
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| - | [[Category: Oxidoreductase]]
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| - | [[Category: Truncated form]]
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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
We previously determined the crystal structures of 1-Cys type selenoprotein MsrA from Clostridium oremlandii (CoMsrA). The overall structure of CoMsrA is unusual, consisting of two domains, the N-terminal catalytic domain and the C-terminal distinct helical domain which is absent from other known MsrA structures. Deletion of the helical domain almost completely abolishes the catalytic activity of CoMsrA. In this study, we determined the crystal structure of the helical domain-deleted (DeltaH-domain) form of CoMsrA at a resolution of 1.76 A. The monomer structure is composed of the central rolled mixed beta-sheet surrounded by alpha-helices. However, there are significant conformational changes in the N- and C-termini and loop regions of the DeltaH-domain protein relative to the catalytic domain structure of full-length CoMsrA. The active site structure in the DeltaH-domain protein completely collapses, thereby causing loss of catalytic activity of the protein. Interestingly, dimer structures are observed in the crystal formed by N-terminus swapping between two molecules. The DeltaH-domain protein primarily exists as a dimer in solution, whereas the full-length CoMsrA exists as a monomer. Collectively, this study provides insight into the structural basis of the essential role of the helical domain of CoMsrA in its catalysis.
Essential role of the C-terminal helical domain in active site formation of selenoprotein MsrA from Clostridium oremlandii.,Lee EH, Lee K, Hwang KY, Kim HY PLoS One. 2015 Feb 18;10(2):e0117836. doi: 10.1371/journal.pone.0117836., eCollection 2015. PMID:25692691[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lee EH, Lee K, Hwang KY, Kim HY. Essential role of the C-terminal helical domain in active site formation of selenoprotein MsrA from Clostridium oremlandii. PLoS One. 2015 Feb 18;10(2):e0117836. doi: 10.1371/journal.pone.0117836., eCollection 2015. PMID:25692691 doi:http://dx.doi.org/10.1371/journal.pone.0117836
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