View source for 4ciy


==Crystal structure of Mycobacterium tuberculosis type 2 dehydroquinase in complex with (1R,4R,5R)-1,4,5-trihydroxy-3-((1R)-1-hydroxy-2- phenyl)ethylcyclohex-2-en-1-carboxylic acid==
<StructureSection load='4ciy' size='340' side='right'caption='[[4ciy]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ciy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CIY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CIY 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NDY:(1R,4R,5R)-1,4,5-TRIHYDROXY-3-[(1R)-1-HYDROXY-2-PHENYL]ETHYLCYCLOHEX-2-ENE-1-CARBOXYLIC+ACID'>NDY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4ciy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ciy OCA], [https://pdbe.org/4ciy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ciy RCSB], [https://www.ebi.ac.uk/pdbsum/4ciy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ciy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AROQ_MYCTU AROQ_MYCTU] Catalyzes a trans-dehydration via an enolate intermediate (By similarity).[HAMAP-Rule:MF_00169]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Structural and computational studies to explore the WAT1 binding pocket in the structure-based design of inhibitors against the type II dehydroquinase (DHQ2) enzyme are reported. The crystal structures of DHQ2 from M. tuberculosis in complex with four of the reported compounds are described. The electrostatic interaction observed between the guanidinium group of the essential arginine and the carboxylate group of one of the inhibitors in the reported crystal structures supports the recently suggested role of this arginine as the residue that triggers the release of the product from the active site. The results of the structural and molecular dynamics simulation studies revealed that the inhibitory potency is favored by promoting interactions with WAT1 and the residues located within this pocket and, more importantly, by avoiding situations where the ligands occupy the WAT1 binding pocket. The new insights can be used to advantage in the structure-based design of inhibitors.

Exploring the Water-Binding Pocket of the Type II Dehydroquinase Enzyme in the Structure-Based Design of Inhibitors.,Blanco B, Sedes A, Peon A, Otero JM, Raaij MJ, Thompson P, Hawkins AR, Gonzalez-Bello C J Med Chem. 2014 Apr 1. PMID:24689821<ref>PMID:24689821</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ciy" style="background-color:#fffaf0;"></div>

==See Also==
*[[Dehydroquinase 3D structures|Dehydroquinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Blanco B]]
[[Category: Gonzalez-Bello C]]
[[Category: Hawkins AR]]
[[Category: Lamb H]]
[[Category: Llamas-Saiz AL]]
[[Category: Otero JM]]
[[Category: Peon A]]
[[Category: Sedes A]]
[[Category: Van Raaij MJ]]