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| | ==Crystal structure of Mxr1 from Saccharomyces cerevisiae in reduced form== | | ==Crystal structure of Mxr1 from Saccharomyces cerevisiae in reduced form== |
| - | <StructureSection load='3pil' size='340' side='right' caption='[[3pil]], [[Resolution|resolution]] 2.04Å' scene=''> | + | <StructureSection load='3pil' size='340' side='right'caption='[[3pil]], [[Resolution|resolution]] 2.04Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3pil]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PIL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PIL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3pil]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PIL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PIL 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></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]] 2.04Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pim|3pim]], [[3pin|3pin]]</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></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MXR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3pil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pil OCA], [https://pdbe.org/3pil PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pil RCSB], [https://www.ebi.ac.uk/pdbsum/3pil PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pil 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>
| + | |
| - | <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=3pil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pil OCA], [http://pdbe.org/3pil PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pil RCSB], [http://www.ebi.ac.uk/pdbsum/3pil PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pil ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MSRA_YEAST MSRA_YEAST]] 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. Also able to reduce dimethyl sulfoxide (DMSO) as well, with DMS as the product. | + | [https://www.uniprot.org/uniprot/MSRA_YEAST MSRA_YEAST] 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. Also able to reduce dimethyl sulfoxide (DMSO) as well, with DMS as the product. |
| | <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: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Chen, Y]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Guo, P C]] | + | [[Category: Chen Y]] |
| - | [[Category: Luo, M]] | + | [[Category: Guo PC]] |
| - | [[Category: Ma, X X]] | + | [[Category: Luo M]] |
| - | [[Category: Shi, W W]] | + | [[Category: Ma XX]] |
| - | [[Category: Tan, X F]] | + | [[Category: Shi WW]] |
| - | [[Category: Zhou, C Z]] | + | [[Category: Tan XF]] |
| - | [[Category: Methionine-s-sulfoxide reductase]]
| + | [[Category: Zhou CZ]] |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
MSRA_YEAST 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. Also able to reduce dimethyl sulfoxide (DMSO) as well, with DMS as the product.
Publication Abstract from PubMed
The methionine S-sulfoxide reductase MsrA catalyzes the reduction of methionine sulfoxide, a ubiquitous reaction depending on the thioredoxin system. To investigate interactions between MsrA and thioredoxin (Trx), we determined the crystal structures of yeast MsrA/Mxr1 in their reduced, oxidized, and Trx2-complexed forms, at 2.03, 1.90, and 2.70 A, respectively. Comparative structure analysis revealed significant conformational changes of the three loops, which form a plastic "cushion" to harbor the electron donor Trx2. The flexible C-terminal loop enabled Mxr1 to access the methionine sulfoxide on various protein substrates. Moreover, the plasticity of the Trx binding site on Mxr1 provides structural insights into the recognition of diverse substrates by a universal catalytic motif of Trx.
Structural plasticity of the thioredoxin recognition site of yeast methionine S-sulfoxide reductase Mxr1.,Ma XX, Guo PC, Shi WW, Luo M, Tan XF, Chen Y, Zhou CZ J Biol Chem. 2011 Apr 15;286(15):13430-7. Epub 2011 Feb 23. PMID:21345799[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ma XX, Guo PC, Shi WW, Luo M, Tan XF, Chen Y, Zhou CZ. Structural plasticity of the thioredoxin recognition site of yeast methionine S-sulfoxide reductase Mxr1. J Biol Chem. 2011 Apr 15;286(15):13430-7. Epub 2011 Feb 23. PMID:21345799 doi:http://dx.doi.org/10.1074/jbc.M110.205161
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