2fls: Difference between revisions

Latest revision as of 09:28, 30 August 2023

Crystal structure of Human Glutaredoxin 2 complexed with glutathione

Structural highlights

2fls is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.05Å
Ligands:	GSH
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

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

References

↑ Lundberg M, Johansson C, Chandra J, Enoksson M, Jacobsson G, Ljung J, Johansson M, Holmgren A. Cloning and expression of a novel human glutaredoxin (Grx2) with mitochondrial and nuclear isoforms. J Biol Chem. 2001 Jul 13;276(28):26269-75. Epub 2001 Apr 10. PMID:11297543 doi:https://dx.doi.org/10.1074/jbc.M011605200
↑ Johansson C, Lillig CH, Holmgren A. Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. J Biol Chem. 2004 Feb 27;279(9):7537-43. Epub 2003 Dec 4. PMID:14676218 doi:https://dx.doi.org/10.1074/jbc.M312719200
↑ Lillig CH, Lonn ME, Enoksson M, Fernandes AP, Holmgren A. Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide. Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13227-32. Epub 2004 Aug 24. PMID:15328416 doi:https://dx.doi.org/10.1073/pnas.0401896101
↑ Enoksson M, Fernandes AP, Prast S, Lillig CH, Holmgren A, Orrenius S. Overexpression of glutaredoxin 2 attenuates apoptosis by preventing cytochrome c release. Biochem Biophys Res Commun. 2005 Feb 18;327(3):774-9. PMID:15649413 doi:https://dx.doi.org/10.1016/j.bbrc.2004.12.067

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Lundberg M, Johansson C, Chandra J, Enoksson M, Jacobsson G, Ljung J, Johansson M, Holmgren A. Cloning and expression of a novel human glutaredoxin (Grx2) with mitochondrial and nuclear isoforms. J Biol Chem. 2001 Jul 13;276(28):26269-75. Epub 2001 Apr 10. PMID:11297543 doi:https://dx.doi.org/10.1074/jbc.M011605200

[2] Johansson C, Lillig CH, Holmgren A. Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. J Biol Chem. 2004 Feb 27;279(9):7537-43. Epub 2003 Dec 4. PMID:14676218 doi:https://dx.doi.org/10.1074/jbc.M312719200

[3] Lillig CH, Lonn ME, Enoksson M, Fernandes AP, Holmgren A. Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide. Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13227-32. Epub 2004 Aug 24. PMID:15328416 doi:https://dx.doi.org/10.1073/pnas.0401896101

[4] Enoksson M, Fernandes AP, Prast S, Lillig CH, Holmgren A, Orrenius S. Overexpression of glutaredoxin 2 attenuates apoptosis by preventing cytochrome c release. Biochem Biophys Res Commun. 2005 Feb 18;327(3):774-9. PMID:15649413 doi:https://dx.doi.org/10.1016/j.bbrc.2004.12.067

[1]

[2]

[3]

[4]

@@ Line 1: / Line 1: @@
-[[Image:2fls.gif|left|200px]]
- {{Structure
+==Crystal structure of Human Glutaredoxin 2 complexed with glutathione==
-|PDB= 2fls |SIZE=350|CAPTION= <scene name='initialview01'>2fls</scene>, resolution 2.05&Aring;
+<StructureSection load='2fls' size='340' side='right'caption='[[2fls]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>
+<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>
-|ACTIVITY=
+</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>
-|GENE= GLRX2, GRX2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
+<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>
+</table>
-'''Crystal structure of Human Glutaredoxin 2 complexed with glutathione'''
+== Function ==
+[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 ==
-==About this Structure==
+[[Image:Consurf_key_small.gif|200px|right]]
-FLS is a [[Single protein]] structure of sequence from [http://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].
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fl/2fls_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=2fls ConSurf].
+<div style="clear:both"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Arrowsmith, C.]]
+[[Category: Arrowsmith C]]
-[[Category: Debreczeni, J.]]
+[[Category: Debreczeni J]]
-[[Category: Edwards, A.]]
+[[Category: Edwards A]]
-[[Category: Gileadi, O.]]
+[[Category: Gileadi O]]
-[[Category: Johansson, C.]]
+[[Category: Johansson C]]
-[[Category: Kavanagh, K L.]]
+[[Category: Kavanagh KL]]
-[[Category: Oppermann, U.]]
+[[Category: Oppermann U]]
-[[Category: SGC, Structural Genomics Consortium.]]
+[[Category: Smee C]]
-[[Category: Smee, C.]]
+[[Category: Sundstrom M]]
-[[Category: Sundstrom, M.]]
+[[Category: Weigelt J]]
-[[Category: Vondelft, F.]]
+[[Category: Von Delft F]]
-[[Category: Weigelt, J.]]
-[[Category: GSH]]
-[[Category: sgc]]
-[[Category: structural genomic]]
-[[Category: structural genomics consortium]]
-[[Category: thioredoxin fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:53:57 2008''

2fls: Difference between revisions

Latest revision as of 09:28, 30 August 2023

Crystal structure of Human Glutaredoxin 2 complexed with glutathione

Structural highlights

Function

Evolutionary Conservation

References

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