5an1: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystallographic structure of the Glutathione S-Transferase from Litopenaeus vannamei complexed with Glutathione== | |||
<StructureSection load='5an1' size='340' side='right' caption='[[5an1]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5an1]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AN1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AN1 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> | |||
<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=5an1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5an1 OCA], [http://pdbe.org/5an1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5an1 RCSB], [http://www.ebi.ac.uk/pdbsum/5an1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5an1 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Glutathione S-transferases (GSTs) are dimeric proteins that play a key role in phase II cellular detoxification. Here, the first crystal structure of a GST class-mu from marine crustacean shrimp Litopenaeus vannamei is reported at a resolution of 2.0 A. The coordinates reported here have the lowest sequence identity with previously reported GSTs class-mu deposited at the Protein Data Bank (PDB), although they have subtle conformational differences. One key feature of GST class-mu from L. vannamei is the active site crevice markedly reduced when it is compared with other GSTs class-mu. This finding together with the chemical change of residues into the cavity (F112 and Y210) points to a particular specialization in which smallest xenobiotics with nonstandard chemical characteristics can be bound to the H-site. This suggests that marine organisms have evolved structural strategies to provide efficient selectivity toward xenobiotics to be disposed of by the phase II detoxification process. | |||
Crystal structure of a class-mu glutathione S-transferase from whiteleg shrimp Litopenaeus vannamei: structural changes in the xenobiotic binding H-site may alter the spectra of molecules bound.,Juarez-Martinez AB, Sotelo-Mundo RR, Rudino-Pinera E J Biochem Mol Toxicol. 2016 Sep 22. doi: 10.1002/jbt.21838. PMID:27717103<ref>PMID:27717103</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5an1" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Glutathione transferase]] | |||
[[Category: Juarez-Martinez, A B]] | |||
[[Category: Rudino-Pinera, E]] | [[Category: Rudino-Pinera, E]] | ||
[[Category: Sotelo-Mundo, R]] | [[Category: Sotelo-Mundo, R]] | ||
[[Category: | [[Category: Disulphide bond gst]] | ||
[[Category: Glutathione]] | |||
[[Category: Mu- class]] | |||
[[Category: Transferase]] | |||
[[Category: Xenobiotic]] | |||
