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| ==Solution structure of murine myristoylated msrA== | | ==Solution structure of murine myristoylated msrA== |
- | <StructureSection load='2l90' size='340' side='right' caption='[[2l90]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | + | <StructureSection load='2l90' size='340' side='right'caption='[[2l90]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2l90]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L90 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L90 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2l90]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L90 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L90 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 21 models</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=10090 LK3 transgenic mice])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2l90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l90 OCA], [https://pdbe.org/2l90 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l90 RCSB], [https://www.ebi.ac.uk/pdbsum/2l90 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l90 ProSAT]</span></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=2l90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l90 OCA], [http://pdbe.org/2l90 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l90 RCSB], [http://www.ebi.ac.uk/pdbsum/2l90 PDBsum]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/MSRA_MOUSE MSRA_MOUSE]] 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/MSRA_MOUSE MSRA_MOUSE] 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: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
- | [[Category: Gruschus, J M]] | + | [[Category: Mus musculus]] |
- | [[Category: Levine, R L]] | + | [[Category: Gruschus JM]] |
- | [[Category: Lim, J]] | + | [[Category: Levine RL]] |
- | [[Category: Piszczek, G]] | + | [[Category: Lim J]] |
- | [[Category: Tjandra, N]] | + | [[Category: Piszczek G]] |
- | [[Category: Oxidoreductase]]
| + | [[Category: Tjandra N]] |
| Structural highlights
Function
MSRA_MOUSE 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 is an essential enzyme in the antioxidant system which scavenges reactive oxygen species through cyclic oxidation and reduction of methionine and methionine sulfoxide. The cytosolic form of the enzyme is myristoylated, but it is not known to translocate to membranes, and the function of myristoylation is not established. We compared the biochemical and biophysical properties of myristoylated and nonmyristoylated mouse methionine sulfoxide reductase A. These were almost identical for both forms of the enzyme, except that the myristoylated form reduced methionine sulfoxide in protein much faster than the nonmyristoylated form. We determined the solution structure of the myristoylated protein and found that the myristoyl group lies in a relatively surface exposed "myristoyl nest." We propose that this structure functions to enhance protein-protein interaction.
Characterization and solution structure of mouse myristoylated methionine sulfoxide reductase a.,Lim JC, Gruschus JM, Ghesquiere B, Kim G, Piszczek G, Tjandra N, Levine RL J Biol Chem. 2012 Jul 20;287(30):25589-95. Epub 2012 Jun 1. PMID:22661718[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lim JC, Gruschus JM, Ghesquiere B, Kim G, Piszczek G, Tjandra N, Levine RL. Characterization and solution structure of mouse myristoylated methionine sulfoxide reductase a. J Biol Chem. 2012 Jul 20;287(30):25589-95. Epub 2012 Jun 1. PMID:22661718 doi:10.1074/jbc.M112.368936
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