5g5e: Difference between revisions
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==Crystallographic structure of the Tau class glutathione S-transferase MiGSTU from mango Mangifera indica L.== | |||
<StructureSection load='5g5e' size='340' side='right' caption='[[5g5e]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5g5e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5G5E FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5g5f|5g5f]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </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=5g5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g5e OCA], [http://pdbe.org/5g5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g5e RCSB], [http://www.ebi.ac.uk/pdbsum/5g5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g5e ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We studied a mango glutathione S-transferase (GST) (Mangifera indica) bound to glutathione (GSH) and S-hexyl glutathione (GSX). This GST Tau class (MiGSTU) had a molecular mass of 25.5 kDa. MiGSTU Michaelis-Menten kinetic constants were determined for their substrates obtaining a Km, Vmax and kcat for CDNB of 0.792 mM, 80.58 mM min-1 and 68.49 s-1 respectively and 0.693 mM, 105.32 mM min-1 and 89.57 s-1, for reduced GSH respectively. MiGSTU had a micromolar affinity towards GSH (5.2 muM) or GSX (7.8 muM). The crystal structure of the MiGSTU in apo or bound to GSH or GSX generated a model that explains the thermodynamic signatures of binding and showed the importance of enthalpic-entropic compensation in ligand binding to Tau-class GST enzymes. | |||
Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics.,Valenzuela-Chavira I, Contreras-Vergara CA, Arvizu-Flores AA, Serrano-Posada H, Lopez-Zavala AA, Garcia-Orozco KD, Hernandez-Paredes J, Rudino-Pinera E, Stojanoff V, Sotelo-Mundo RR, Islas-Osuna MA Biochimie. 2017 Jan 16. pii: S0300-9084(16)30283-8. doi:, 10.1016/j.biochi.2017.01.005. PMID:28104507<ref>PMID:28104507</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5g5e" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Glutathione transferase]] | |||
[[Category: Hernandez-Paredes, J]] | |||
[[Category: Lopez-Zavala, A]] | [[Category: Lopez-Zavala, A]] | ||
[[Category: Serrano-Posada, H]] | |||
[[Category: Sotelo-Mundo, R]] | [[Category: Sotelo-Mundo, R]] | ||
[[Category: | [[Category: Valenzuela-Chavira, I]] | ||
[[Category: | [[Category: Detoxification]] | ||
[[Category: Glutathione s-transferase]] | |||
[[Category: Mango]] | |||
[[Category: Tau class]] | |||
[[Category: Transferase]] | |||
Revision as of 17:51, 1 February 2017
Crystallographic structure of the Tau class glutathione S-transferase MiGSTU from mango Mangifera indica L.
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