2cq9: Difference between revisions

Revision as of 06:59, 1 December 2021

Solution structure of RSGI RUH-044, an N-terminal domain of Glutaredoxin 2 from human cDNA

Structural highlights

2cq9 is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

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

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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 3: / Line 3: @@
 <StructureSection load='2cq9' size='340' side='right'caption='[[2cq9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2cq9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CQ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CQ9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2cq9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CQ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CQ9 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cq9 OCA], [http://pdbe.org/2cq9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cq9 RCSB], [http://www.ebi.ac.uk/pdbsum/2cq9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cq9 ProSAT], [http://www.topsan.org/Proteins/RSGI/2cq9 TOPSAN]</span></td></tr>
+</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=2cq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cq9 OCA], [https://pdbe.org/2cq9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cq9 RCSB], [https://www.ebi.ac.uk/pdbsum/2cq9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cq9 ProSAT], [https://www.topsan.org/Proteins/RSGI/2cq9 TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

2cq9: Difference between revisions

Revision as of 06:59, 1 December 2021

Solution structure of RSGI RUH-044, an N-terminal domain of Glutaredoxin 2 from human cDNA

Structural highlights

Function

Evolutionary Conservation

References

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