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- | [[Image:2hsy.jpg|left|200px]] | |
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- | <!-- | + | ==Solution structure of Thioredoxin 2 from Saccharomyces cerevisiae== |
- | The line below this paragraph, containing "STRUCTURE_2hsy", creates the "Structure Box" on the page.
| + | <StructureSection load='2hsy' size='340' side='right'caption='[[2hsy]]' scene=''> |
- | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[2hsy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HSY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HSY FirstGlance]. <br> |
- | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2hsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hsy OCA], [https://pdbe.org/2hsy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hsy RCSB], [https://www.ebi.ac.uk/pdbsum/2hsy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hsy ProSAT]</span></td></tr> |
- | {{STRUCTURE_2hsy| PDB=2hsy | SCENE= }}
| + | </table> |
| + | == Function == |
| + | [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> |
| + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> |
| + | <jmolCheckbox> |
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hs/2hsy_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| + | </jmolCheckbox> |
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hsy ConSurf]. |
| + | <div style="clear:both"></div> |
| | | |
- | '''Solution structure of Thioredoxin 2 from Saccharomyces cerevisiae'''
| + | ==See Also== |
- | | + | *[[Thioredoxin 3D structures|Thioredoxin 3D structures]] |
- | | + | == References == |
- | ==About this Structure== | + | <references/> |
- | 2HSY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HSY OCA].
| + | __TOC__ |
- | | + | </StructureSection> |
- | ==Reference== | + | [[Category: Large Structures]] |
- | NMR solution structure of the reduced form of thioredoxin 2 from Saccharomyces cerevisiae., Amorim GC, Pinheiro AS, Netto LE, Valente AP, Almeida FC, J Biomol NMR. 2007 May;38(1):99-104. Epub 2007 Mar 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17340205 17340205]
| + | |
| [[Category: Saccharomyces cerevisiae]] | | [[Category: Saccharomyces cerevisiae]] |
- | [[Category: Single protein]]
| + | [[Category: Almeida FCL]] |
- | [[Category: Almeida, F C.L.]] | + | [[Category: Amorim GC]] |
- | [[Category: Amorim, G C.]] | + | [[Category: Valente AP]] |
- | [[Category: Valente, A P.]] | + | |
- | [[Category: Oxidoreductase]]
| + | |
- | [[Category: Thioredoxin]]
| + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:40:16 2008''
| + | |
| 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]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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
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