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| | ==Crystal structure of GSH-bound cGrx2/C15S== | | ==Crystal structure of GSH-bound cGrx2/C15S== |
| - | <StructureSection load='4tr1' size='340' side='right' caption='[[4tr1]], [[Resolution|resolution]] 1.58Å' scene=''> | + | <StructureSection load='4tr1' size='340' side='right'caption='[[4tr1]], [[Resolution|resolution]] 1.58Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4tr1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Alkoo Alkoo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TR1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TR1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4tr1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkaliphilus_oremlandii_OhILAs Alkaliphilus oremlandii OhILAs]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TR1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=CSU:CYSTEINE-S-SULFONIC+ACID'>CSU</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=CSU:CYSTEINE-S-SULFONIC+ACID'>CSU</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=4tr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tr1 OCA], [https://pdbe.org/4tr1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tr1 RCSB], [https://www.ebi.ac.uk/pdbsum/4tr1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tr1 ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tr0|4tr0]]</td></tr>
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| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Clos_2422 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=350688 ALKOO])</td></tr>
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| - | <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=4tr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tr1 OCA], [http://pdbe.org/4tr1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tr1 RCSB], [http://www.ebi.ac.uk/pdbsum/4tr1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tr1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A8MJH2_ALKOO A8MJH2_ALKOO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alkoo]] | + | [[Category: Alkaliphilus oremlandii OhILAs]] |
| - | [[Category: Hwang, K Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Lee, E H]] | + | [[Category: Hwang KY]] |
| - | [[Category: Glutaredoxin]] | + | [[Category: Lee EH]] |
| - | [[Category: Gsh]]
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| - | [[Category: Oxidoreductase]]
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| Structural highlights
Function
A8MJH2_ALKOO
Publication Abstract from PubMed
Glutaredoxin (Grx) is a major redox enzyme that reduces disulfide bonds using glutathione (GSH) as an electron donor. The anaerobic bacterium Clostridium oremlandii possesses a selenocysteine-containing Grx (cGrx1) and a cysteine-containing homolog (cGrx2). Here, the crystal structure of the GSSG-bound form of cGrx2 was determined for the first time at a resolution of 1.95 A. In addition, its monothiol variant cGrx2/C15S in complex with GSH was also determined at a resolution of 1.58 A. cGrx2 is a monomeric protein with an overall structure that consists of the typical thioredoxin fold composed of four alpha-helices and four beta-strands. Two ligands, GSH and GSSG, share a conserved binding site consisting of CPYC, TVP, and CDD motifs. The cysteinyl and gamma-glutamyl moieties show similar binding interactions in the two structures, whereas the glycine moiety shows different interactions. Interestingly, the structures revealed that only one GSH moiety of GSSG is sufficient for its binding to the protein. The GSSG-bound structure of cGrx2 was obtained as an oxidized form with a disulfide bond at the CPYC motif. Comparison of the GSH-binding mode in cGrx2 to other known Grxs revealed similarities as well as some diversity.
The GSH- and GSSG-bound structures of glutaredoxin from Clostridium oremlandii.,Lee EH, Kim HY, Hwang KY Arch Biochem Biophys. 2014 Sep 9. pii: S0003-9861(14)00320-8. doi:, 10.1016/j.abb.2014.09.001. PMID:25218089[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lee EH, Kim HY, Hwang KY. The GSH- and GSSG-bound structures of glutaredoxin from Clostridium oremlandii. Arch Biochem Biophys. 2014 Sep 9. pii: S0003-9861(14)00320-8. doi:, 10.1016/j.abb.2014.09.001. PMID:25218089 doi:http://dx.doi.org/10.1016/j.abb.2014.09.001
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