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| | ==Crystal structure of Mxr1 from Saccharomyces cerevisiae in complex with Trx2== | | ==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=''> | + | <StructureSection load='3pin' size='340' side='right'caption='[[3pin]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == 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> | + | <table><tr><td colspan='2'>[[3pin]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3PIN FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pil|3pil]], [[3pim|3pim]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3pil|3pil]], [[3pim|3pim]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRX2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), MXR1 ([https://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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptide-methionine_(S)-S-oxide_reductase Peptide-methionine (S)-S-oxide reductase], with EC number [https://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://pdbe.org/3pin PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pin RCSB], [http://www.ebi.ac.uk/pdbsum/3pin PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pin ProSAT]</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=3pin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pin OCA], [https://pdbe.org/3pin PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pin RCSB], [https://www.ebi.ac.uk/pdbsum/3pin PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pin ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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. | + | [[https://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> [[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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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Thioredoxin|Thioredoxin]] | + | *[[Thioredoxin 3D structures|Thioredoxin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Atcc 18824]] | | [[Category: Atcc 18824]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Chen, Y]] | | [[Category: Chen, Y]] |
| | [[Category: Guo, P C]] | | [[Category: Guo, P C]] |
| Structural highlights
Function
[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.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [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[11]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schwenn JD, Krone FA, Husmann K. Yeast PAPS reductase: properties and requirements of the purified enzyme. Arch Microbiol. 1988;150(4):313-9. PMID:3060034
- ↑ Xu Z, Mayer A, Muller E, Wickner W. A heterodimer of thioredoxin and I(B)2 cooperates with Sec18p (NSF) to promote yeast vacuole inheritance. J Cell Biol. 1997 Jan 27;136(2):299-306. PMID:9015301
- ↑ Xu Z, Sato K, Wickner W. LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion. Cell. 1998 Jun 26;93(7):1125-34. PMID:9657146
- ↑ Park SG, Cha MK, Jeong W, Kim IH. Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae. J Biol Chem. 2000 Feb 25;275(8):5723-32. PMID:10681558
- ↑ Lee J, Spector D, Godon C, Labarre J, Toledano MB. A new antioxidant with alkyl hydroperoxide defense properties in yeast. J Biol Chem. 1999 Feb 19;274(8):4537-44. PMID:9988687
- ↑ Delaunay A, Isnard AD, Toledano MB. H2O2 sensing through oxidation of the Yap1 transcription factor. EMBO J. 2000 Oct 2;19(19):5157-66. PMID:11013218 doi:http://dx.doi.org/10.1093/emboj/19.19.5157
- ↑ Delaunay A, Pflieger D, Barrault MB, Vinh J, Toledano MB. A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation. Cell. 2002 Nov 15;111(4):471-81. PMID:12437921
- ↑ Trotter EW, Grant CM. Thioredoxins are required for protection against a reductive stress in the yeast Saccharomyces cerevisiae. Mol Microbiol. 2002 Nov;46(3):869-78. PMID:12410842
- ↑ Grant CM. Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions. Mol Microbiol. 2001 Feb;39(3):533-41. PMID:11169096
- ↑ Elazar Z, Scherz-Shouval R, Shorer H. Involvement of LMA1 and GATE-16 family members in intracellular membrane dynamics. Biochim Biophys Acta. 2003 Aug 18;1641(2-3):145-56. PMID:12914955
- ↑ 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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