2fls

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Current revision (09:28, 30 August 2023) (edit) (undo)
 
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<StructureSection load='2fls' size='340' side='right'caption='[[2fls]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
<StructureSection load='2fls' size='340' side='right'caption='[[2fls]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2fls]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FLS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2fls]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FLS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLRX2, GRX2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></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=2fls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fls OCA], [https://pdbe.org/2fls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fls RCSB], [https://www.ebi.ac.uk/pdbsum/2fls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fls 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=2fls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fls OCA], [https://pdbe.org/2fls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fls RCSB], [https://www.ebi.ac.uk/pdbsum/2fls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fls ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/GLRX2_HUMAN GLRX2_HUMAN]] Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.<ref>PMID:11297543</ref> <ref>PMID:14676218</ref> <ref>PMID:15328416</ref> <ref>PMID:15649413</ref>
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[https://www.uniprot.org/uniprot/GLRX2_HUMAN GLRX2_HUMAN] Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.<ref>PMID:11297543</ref> <ref>PMID:14676218</ref> <ref>PMID:15328416</ref> <ref>PMID:15649413</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>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arrowsmith, C]]
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[[Category: Arrowsmith C]]
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[[Category: Debreczeni, J]]
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[[Category: Debreczeni J]]
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[[Category: Delft, F von]]
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[[Category: Edwards A]]
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[[Category: Edwards, A]]
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[[Category: Gileadi O]]
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[[Category: Gileadi, O]]
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[[Category: Johansson C]]
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[[Category: Johansson, C]]
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[[Category: Kavanagh KL]]
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[[Category: Kavanagh, K L]]
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[[Category: Oppermann U]]
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[[Category: Oppermann, U]]
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[[Category: Smee C]]
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[[Category: Structural genomic]]
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[[Category: Sundstrom M]]
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[[Category: Smee, C]]
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[[Category: Weigelt J]]
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[[Category: Sundstrom, M]]
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[[Category: Von Delft F]]
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[[Category: Weigelt, J]]
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[[Category: Oxidoreductase]]
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[[Category: Sgc]]
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[[Category: Thioredoxin fold]]
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Current revision

Crystal structure of Human Glutaredoxin 2 complexed with glutathione

PDB ID 2fls

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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