5x5m

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "5x5m" [edit=sysop:move=sysop])
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5x5m is ON HOLD until Paper Publication
+
==Crystal structure of a hydrolase encoded by lin2189 from Listeria innocua==
 +
<StructureSection load='5x5m' size='340' side='right' caption='[[5x5m]], [[Resolution|resolution]] 1.21&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[5x5m]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X5M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X5M FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7YU:(+)-Yatakemycin'>7YU</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene></td></tr>
 +
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x5r|5x5r]]</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=5x5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x5m OCA], [http://pdbe.org/5x5m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x5m RCSB], [http://www.ebi.ac.uk/pdbsum/5x5m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x5m ProSAT]</span></td></tr>
 +
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
GyrI-like proteins are widely distributed in prokaryotes and eukaryotes, and recognized as small-molecule binding proteins. Here, we identify a subfamily of these proteins as cyclopropanoid cyclopropyl hydrolases (CCHs) that can catalyze the hydrolysis of the potent DNA-alkylating agents yatakemycin (YTM) and CC-1065. Co-crystallography and molecular dynamics simulation analyses reveal that these CCHs share a conserved aromatic cage for the hydrolytic activity. Subsequent cytotoxic assays confirm that CCHs are able to protect cells against YTM. Therefore, our findings suggest that the evolutionarily conserved GyrI-like proteins confer cellular protection against diverse xenobiotics via not only binding, but also catalysis.
-
Authors: Zhang, J.
+
GyrI-like proteins catalyze cyclopropanoid hydrolysis to confer cellular protection.,Yuan H, Zhang J, Cai Y, Wu S, Yang K, Chan HCS, Huang W, Jin WB, Li Y, Yin Y, Igarashi Y, Yuan S, Zhou J, Tang GL Nat Commun. 2017 Nov 14;8(1):1485. doi: 10.1038/s41467-017-01508-1. PMID:29133784<ref>PMID:29133784</ref>
-
Description: Crystal structure of a hydrolase encoded by lin2189 from Listeria innocua
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
 +
<div class="pdbe-citations 5x5m" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Zhang, J]]
[[Category: Zhang, J]]
 +
[[Category: Hydrolase]]
 +
[[Category: Hydrolase-antibiotic complex]]

Revision as of 07:19, 6 December 2017

Crystal structure of a hydrolase encoded by lin2189 from Listeria innocua

5x5m, resolution 1.21Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools