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| | <StructureSection load='2hqm' size='340' side='right'caption='[[2hqm]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='2hqm' size='340' side='right'caption='[[2hqm]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2hqm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HQM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HQM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2hqm]] 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=2HQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HQM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </span></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=2hqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hqm OCA], [http://pdbe.org/2hqm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hqm RCSB], [http://www.ebi.ac.uk/pdbsum/2hqm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hqm 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=2hqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hqm OCA], [https://pdbe.org/2hqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hqm RCSB], [https://www.ebi.ac.uk/pdbsum/2hqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hqm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GSHR_YEAST GSHR_YEAST]] Maintains high levels of reduced glutathione in the cytosol. | + | [[https://www.uniprot.org/uniprot/GSHR_YEAST GSHR_YEAST]] Maintains high levels of reduced glutathione in the cytosol. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
2hqm is a 2 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , |
| Activity: | Glutathione-disulfide reductase, with EC number 1.8.1.7 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[GSHR_YEAST] Maintains high levels of reduced glutathione in the cytosol.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Yeast glutathione (GSH) reductase Glr1 is a dimeric flavo-oxidoreductase involved in cytoplasmic and mitochondrial redox regulatory systems. It reduces the oxidized GSH GSSG to the reduced form, GSH with NADPH as electron donor and FAD as coenzyme. Crystal structures and enzymatic mechanisms of GSH reductases from Escherichia coli and Homo sapiens have been well investigated, whereas the structural properties of yeast Glr1 remain unknown. Herein, we overexpressed Saccharomyces cerevisiae Glr1 in Pichia pastoris GS115 and determined its crystal structure at 2.40 A resolution. Although the overall structure and the active site are much conserved, obvious variety was found at the interface of Glr1 monomers when superimposed against the homolog from E. coli or human. The nonconserved C239 is exposed to the solvent and accessible to GSH or GSSG enriched in a microenvironment around the Glr1 molecules, leading to the partial and transient glutathionylation, as primarily identified from the 2Fo-Fc electron density map and further confirmed by biochemical assays. Meanwhile N278 at the vicinity of NADP-binding pocket was artificially glycosylated when heterogeneously overexpressed in P. pastoris. The highly motile oligosaccharide chain linked to N278 of the recombinant Glr1 interferes with the entry of NADPH, which results in a dramatic increase of Km for NAPDH and a significant decrease of turnover number, when compared with the native protein.
Crystal structure of glutathione reductase Glr1 from the yeast Saccharomyces cerevisiae.,Yu J, Zhou CZ Proteins. 2007 Sep 1;68(4):972-9. PMID:17554778[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yu J, Zhou CZ. Crystal structure of glutathione reductase Glr1 from the yeast Saccharomyces cerevisiae. Proteins. 2007 Sep 1;68(4):972-9. PMID:17554778 doi:10.1002/prot.21354
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