6du7
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Glutathione reductase from Streptococcus pneumoniae== | |
| + | <StructureSection load='6du7' size='340' side='right' caption='[[6du7]], [[Resolution|resolution]] 2.56Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6du7]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DU7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DU7 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=SCN:THIOCYANATE+ION'>SCN</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='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=6du7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6du7 OCA], [http://pdbe.org/6du7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6du7 RCSB], [http://www.ebi.ac.uk/pdbsum/6du7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6du7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The glutathione reductase (GR) from Streptococcus pneumoniae is a flavoenzyme that catalyzes the reduction of oxidized glutathione (GSSG) to its reduced form (GSH) in the cytoplasm of this bacterium. The maintenance of an intracellular pool of GSH is critical for the detoxification of reactive oxygen and nitrogen species and for intracellular metal tolerance to ions such as zinc. Here, S. pneumoniae GR (SpGR) was overexpressed and purified and its crystal structure determined at 2.56 A resolution. SpGR shows overall structural similarity to other characterized GRs, with a dimeric structure that includes an antiparallel beta-sheet at the dimer interface. This observation, in conjunction with comparisons with the interface structures of other GR enzymes, allows the classification of these enzymes into three classes. Analyses of the kinetic properties of SpGR revealed a significantly higher value for Km(GSSG) (231.2 +/- 24.7 microM) in comparison to other characterized GR enzymes. | ||
| - | + | The structure and activity of the glutathione reductase from Streptococcus pneumoniae.,Sikanyika M, Aragao D, McDevitt CA, Maher MJ Acta Crystallogr F Struct Biol Commun. 2019 Jan 1;75(Pt 1):54-61. doi:, 10.1107/S2053230X18016527. Epub 2019 Jan 1. PMID:30605126<ref>PMID:30605126</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6du7" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Glutathione-disulfide reductase]] | ||
| + | [[Category: Maher, M J]] | ||
[[Category: Sikanyika, M]] | [[Category: Sikanyika, M]] | ||
| - | [[Category: | + | [[Category: Glutathione reductase]] |
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Streptococcus pneumoniae]] | ||
Revision as of 12:06, 16 January 2019
Glutathione reductase from Streptococcus pneumoniae
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