3rbt: Difference between revisions
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[[ | ==Crystal structure of glutathione S-transferase Omega 3 from the silkworm Bombyx mori== | ||
<StructureSection load='3rbt' size='340' side='right' caption='[[3rbt]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3rbt]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RBT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RBT FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene><br> | |||
<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rbt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rbt RCSB], [http://www.ebi.ac.uk/pdbsum/3rbt PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Glutathione transferases (GSTs) are ubiquitous detoxification enzymes that conjugate hydrophobic xenobiotics with reduced glutathione. The silkworm Bombyx mori encodes four isoforms of GST Omega (GSTO), featured with a catalytic cysteine, except that bmGSTO3-3 has an asparagine substitution of this catalytic residue. Here, we determined the 2.20-A crystal structure of bmGSTO3-3, which shares a typical GST overall structure. However, the extended C-terminal segment that exists in all the four bmGSTOs occupies the G-site of bmGSTO3-3 and makes it unworkable, as shown by the activity assays. Upon mutation of Asn29 to Cys and truncation of the C-terminal segment, the in vitro GST activity of bmGSTO3-3 could be restored. These findings provided structural insights into the activity regulation of GSTOs. | |||
Structure-guided activity restoration of the silkworm glutathione transferase Omega GSTO3-3.,Chen BY, Ma XX, Guo PC, Tan X, Li WF, Yang JP, Zhang NN, Chen Y, Xia Q, Zhou CZ J Mol Biol. 2011 Sep 16;412(2):204-11. Epub 2011 Jul 22. PMID:21816159<ref>PMID:21816159</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Glutathione S-transferase|Glutathione S-transferase]] | |||
== | == References == | ||
[[ | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bombyx mori]] | [[Category: Bombyx mori]] | ||
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
Revision as of 06:52, 25 June 2014
Crystal structure of glutathione S-transferase Omega 3 from the silkworm Bombyx mori
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