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2fa4
From Proteopedia
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| - | [[Image:2fa4.png|left|200px]] | ||
| - | + | ==Crystal Structure of Oxidized Form from Saccharomyces cerevisiae== | |
| - | + | <StructureSection load='2fa4' size='340' side='right'caption='[[2fa4]], [[Resolution|resolution]] 2.38Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2fa4]] 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=2FA4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FA4 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ert|1ert]], [[1ep7|1ep7]]</div></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=2fa4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fa4 OCA], [https://pdbe.org/2fa4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fa4 RCSB], [https://www.ebi.ac.uk/pdbsum/2fa4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fa4 ProSAT]</span></td></tr> |
| - | [[2fa4]] is a 2 chain structure | + | </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/fa/2fa4_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=2fa4 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Thioredoxin|Thioredoxin]] | + | *[[Thioredoxin 3D structures|Thioredoxin 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: Bao, R | + | [[Category: Atcc 18824]] |
| - | [[Category: Chen, Y | + | [[Category: Large Structures]] |
| - | [[Category: Tang, Y J | + | [[Category: Bao, R]] |
| - | [[Category: Zhou, C Z | + | [[Category: Chen, Y]] |
| + | [[Category: Tang, Y J]] | ||
| + | [[Category: Zhou, C Z]] | ||
[[Category: Alpha/beta sandwich]] | [[Category: Alpha/beta sandwich]] | ||
[[Category: Dimer]] | [[Category: Dimer]] | ||
[[Category: Electron transport]] | [[Category: Electron transport]] | ||
Current revision
Crystal Structure of Oxidized Form from Saccharomyces cerevisiae
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