2fa4: Difference between revisions

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<StructureSection load='2fa4' size='340' side='right'caption='[[2fa4]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
<StructureSection load='2fa4' size='340' side='right'caption='[[2fa4]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
== Structural highlights ==
== 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>
<table><tr><td colspan='2'>[[2fa4]] is a 2 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=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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.38&#8491;</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>
<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>
</table>
</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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fa/2fa4_consurf.spt"</scriptWhenChecked>
     <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>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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==See Also==
==See Also==
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bao, R]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Chen, Y]]
[[Category: Bao R]]
[[Category: Tang, Y J]]
[[Category: Chen Y]]
[[Category: Zhou, C Z]]
[[Category: Tang YJ]]
[[Category: Alpha/beta sandwich]]
[[Category: Zhou CZ]]
[[Category: Dimer]]
[[Category: Electron transport]]

Latest revision as of 03:55, 21 November 2024

Crystal Structure of Oxidized Form from Saccharomyces cerevisiaeCrystal Structure of Oxidized Form from Saccharomyces cerevisiae

Structural highlights

2fa4 is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.38Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2fa4, resolution 2.38Å

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