3pin
From Proteopedia
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| - | + | ==Crystal structure of Mxr1 from Saccharomyces cerevisiae in complex with Trx2== | |
| - | + | <StructureSection load='3pin' size='340' side='right' caption='[[3pin]], [[Resolution|resolution]] 2.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3pin]] 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=3PIN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PIN FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pil|3pil]], [[3pim|3pim]]</td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRX2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), MXR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3pin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pin OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pin RCSB], [http://www.ebi.ac.uk/pdbsum/3pin PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/TRX2_YEAST TRX2_YEAST]] Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl-hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism. Through its capacity to inactivate the stress response transcription factor YAP1 and its regulator the hydroperoxide stress sensor HYR1, it is involved in feedback regulation of stress response gene expression upon oxidative stress.<ref>PMID:3060034</ref> <ref>PMID:9015301</ref> <ref>PMID:9657146</ref> <ref>PMID:10681558</ref> <ref>PMID:9988687</ref> <ref>PMID:11013218</ref> <ref>PMID:12437921</ref> <ref>PMID:12410842</ref> <ref>PMID:11169096</ref> <ref>PMID:12914955</ref> [[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. | [[http://www.uniprot.org/uniprot/TRX2_YEAST TRX2_YEAST]] Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl-hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism. Through its capacity to inactivate the stress response transcription factor YAP1 and its regulator the hydroperoxide stress sensor HYR1, it is involved in feedback regulation of stress response gene expression upon oxidative stress.<ref>PMID:3060034</ref> <ref>PMID:9015301</ref> <ref>PMID:9657146</ref> <ref>PMID:10681558</ref> <ref>PMID:9988687</ref> <ref>PMID:11013218</ref> <ref>PMID:12437921</ref> <ref>PMID:12410842</ref> <ref>PMID:11169096</ref> <ref>PMID:12914955</ref> [[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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:21345799</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
==See Also== | ==See Also== | ||
*[[Thioredoxin|Thioredoxin]] | *[[Thioredoxin|Thioredoxin]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Atcc 18824]] | [[Category: Atcc 18824]] | ||
| - | [[Category: Chen, Y | + | [[Category: Chen, Y]] |
| - | [[Category: Guo, P C | + | [[Category: Guo, P C]] |
| - | [[Category: Luo, M | + | [[Category: Luo, M]] |
| - | [[Category: Ma, X X | + | [[Category: Ma, X X]] |
| - | [[Category: Shi, W W | + | [[Category: Shi, W W]] |
| - | [[Category: Tan, X F | + | [[Category: Tan, X F]] |
| - | [[Category: Zhou, C Z | + | [[Category: Zhou, C Z]] |
[[Category: Electron transport-oxidoreductase complex]] | [[Category: Electron transport-oxidoreductase complex]] | ||
[[Category: Methionine-s-sulfoxide reductase]] | [[Category: Methionine-s-sulfoxide reductase]] | ||
[[Category: Thioredoxin]] | [[Category: Thioredoxin]] | ||
Revision as of 14:33, 25 December 2014
Crystal structure of Mxr1 from Saccharomyces cerevisiae in complex with Trx2
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