View source for 5kej


==Crystallographic structure of the Tau class glutathione S-transferase MiGSTU in complex with S-hexyl-glutathione==
<StructureSection load='5kej' size='340' side='right'caption='[[5kej]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5kej]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mangifera_indica Mangifera indica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KEJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTX:S-HEXYLGLUTATHIONE'>GTX</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=5kej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kej OCA], [https://pdbe.org/5kej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kej RCSB], [https://www.ebi.ac.uk/pdbsum/5kej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kej ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1P8NWC2_MANIN A0A1P8NWC2_MANIN] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5kej" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mangifera indica]]
[[Category: Hernandez-Paredes J]]
[[Category: Lopez-Zavala A]]
[[Category: Serrano-Posada H]]
[[Category: Sotelo-Mundo R]]
[[Category: Valenzuela-Chavira I]]