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| | <StructureSection load='3cmi' size='340' side='right'caption='[[3cmi]], [[Resolution|resolution]] 2.02Å' scene=''> | | <StructureSection load='3cmi' size='340' side='right'caption='[[3cmi]], [[Resolution|resolution]] 2.02Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3cmi]] is a 1 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=3CMI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CMI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3cmi]] is a 1 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=3CMI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CMI FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HYR1, GPX3, ORP1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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]] 2.02Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peroxiredoxin Peroxiredoxin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.15 1.11.1.15] </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=3cmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cmi OCA], [https://pdbe.org/3cmi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cmi RCSB], [https://www.ebi.ac.uk/pdbsum/3cmi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cmi 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=3cmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cmi OCA], [https://pdbe.org/3cmi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cmi RCSB], [https://www.ebi.ac.uk/pdbsum/3cmi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cmi ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GPX3_YEAST GPX3_YEAST]] Involved in oxidative stress response and redox homeostasis. Functions as a sensor and transducer of hydroperoxide stress. In response to hydroperoxide stress it oxidizes (activates) the transcription activator YAP1, which is involved in transcription activation of genes of the oxidative stress response pathway. May also play a direct role in hydroperoxide scavenging, being the most active of three closely related S.cerevisiae peroxiredoxins (GPX1, GPX2, and HYP1/GPX3) with respect to peroxide and lipid hydroperoxide reduction. The three enzymes are not required for the glutaredoxin-mediated antioxidant function. In the presence of peroxides, HYP1 is directly oxidized at Cys-36 to form a cysteine sulfenic acid (-SOH). Cys-36-SOH then forms either an intramolecular disulfide bond (Cys-36 with Cys-82) or a transient, intermolecular disulfide bond with 'Cys-598' of YAP1, which is further resolved into a YAP1 intramolecular disulfide bond ('Cys-303' with 'Cys-598') and a reduced Cys-36 in HYP1/GPX3.<ref>PMID:9315326</ref> <ref>PMID:10480913</ref> <ref>PMID:11445588</ref> <ref>PMID:11875065</ref> <ref>PMID:12437921</ref> <ref>PMID:12517450</ref> <ref>PMID:12743123</ref> <ref>PMID:14556853</ref>
| + | [https://www.uniprot.org/uniprot/GPX3_YEAST GPX3_YEAST] Involved in oxidative stress response and redox homeostasis. Functions as a sensor and transducer of hydroperoxide stress. In response to hydroperoxide stress it oxidizes (activates) the transcription activator YAP1, which is involved in transcription activation of genes of the oxidative stress response pathway. May also play a direct role in hydroperoxide scavenging, being the most active of three closely related S.cerevisiae peroxiredoxins (GPX1, GPX2, and HYP1/GPX3) with respect to peroxide and lipid hydroperoxide reduction. The three enzymes are not required for the glutaredoxin-mediated antioxidant function. In the presence of peroxides, HYP1 is directly oxidized at Cys-36 to form a cysteine sulfenic acid (-SOH). Cys-36-SOH then forms either an intramolecular disulfide bond (Cys-36 with Cys-82) or a transient, intermolecular disulfide bond with 'Cys-598' of YAP1, which is further resolved into a YAP1 intramolecular disulfide bond ('Cys-303' with 'Cys-598') and a reduced Cys-36 in HYP1/GPX3.<ref>PMID:9315326</ref> <ref>PMID:10480913</ref> <ref>PMID:11445588</ref> <ref>PMID:11875065</ref> <ref>PMID:12437921</ref> <ref>PMID:12517450</ref> <ref>PMID:12743123</ref> <ref>PMID:14556853</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peroxiredoxin]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: He, Y X]] | + | [[Category: He YX]] |
| - | [[Category: Yu, J]] | + | [[Category: Yu J]] |
| - | [[Category: Zhang, W J.Z]] | + | [[Category: Zhang WJZ]] |
| - | [[Category: Zhou, C Z]] | + | [[Category: Zhou CZ]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Peroxidase]]
| + | |
| - | [[Category: Redox-active center]]
| + | |
| - | [[Category: Thioredoxin-like fold]]
| + | |
| Structural highlights
Function
GPX3_YEAST Involved in oxidative stress response and redox homeostasis. Functions as a sensor and transducer of hydroperoxide stress. In response to hydroperoxide stress it oxidizes (activates) the transcription activator YAP1, which is involved in transcription activation of genes of the oxidative stress response pathway. May also play a direct role in hydroperoxide scavenging, being the most active of three closely related S.cerevisiae peroxiredoxins (GPX1, GPX2, and HYP1/GPX3) with respect to peroxide and lipid hydroperoxide reduction. The three enzymes are not required for the glutaredoxin-mediated antioxidant function. In the presence of peroxides, HYP1 is directly oxidized at Cys-36 to form a cysteine sulfenic acid (-SOH). Cys-36-SOH then forms either an intramolecular disulfide bond (Cys-36 with Cys-82) or a transient, intermolecular disulfide bond with 'Cys-598' of YAP1, which is further resolved into a YAP1 intramolecular disulfide bond ('Cys-303' with 'Cys-598') and a reduced Cys-36 in HYP1/GPX3.[1] [2] [3] [4] [5] [6] [7] [8]
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
- ↑ Ursini F, Maiorino M, Roveri A. Phospholipid hydroperoxide glutathione peroxidase (PHGPx): more than an antioxidant enzyme? Biomed Environ Sci. 1997 Sep;10(2-3):327-32. PMID:9315326
- ↑ Inoue Y, Matsuda T, Sugiyama K, Izawa S, Kimura A. Genetic analysis of glutathione peroxidase in oxidative stress response of Saccharomyces cerevisiae. J Biol Chem. 1999 Sep 17;274(38):27002-9. PMID:10480913
- ↑ Avery AM, Avery SV. Saccharomyces cerevisiae expresses three phospholipid hydroperoxide glutathione peroxidases. J Biol Chem. 2001 Sep 7;276(36):33730-5. Epub 2001 Jul 9. PMID:11445588 doi:http://dx.doi.org/10.1074/jbc.M105672200
- ↑ Collinson EJ, Wheeler GL, Garrido EO, Avery AM, Avery SV, Grant CM. The yeast glutaredoxins are active as glutathione peroxidases. J Biol Chem. 2002 May 10;277(19):16712-7. Epub 2002 Mar 1. PMID:11875065 doi:http://dx.doi.org/10.1074/jbc.M111686200
- ↑ 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
- ↑ Wood ZA, Schroder E, Robin Harris J, Poole LB. Structure, mechanism and regulation of peroxiredoxins. Trends Biochem Sci. 2003 Jan;28(1):32-40. PMID:12517450
- ↑ Veal EA, Ross SJ, Malakasi P, Peacock E, Morgan BA. Ybp1 is required for the hydrogen peroxide-induced oxidation of the Yap1 transcription factor. J Biol Chem. 2003 Aug 15;278(33):30896-904. Epub 2003 May 12. PMID:12743123 doi:http://dx.doi.org/10.1074/jbc.M303542200
- ↑ Azevedo D, Tacnet F, Delaunay A, Rodrigues-Pousada C, Toledano MB. Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals signaling. Free Radic Biol Med. 2003 Oct 15;35(8):889-900. PMID:14556853
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