View source for 4cno


==Structure of the Salmonella typhi Type I dehydroquinase inhibited by a 3-dehydroquinic acid derivative==
<StructureSection load='4cno' size='340' side='right'caption='[[4cno]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4cno]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhi Salmonella enterica subsp. enterica serovar Typhi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CNO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CNO 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]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9PY:(2R)-2-METHYL-3-DEHYDROQUINIC+ACID'>9PY</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=4cno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cno OCA], [https://pdbe.org/4cno PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cno RCSB], [https://www.ebi.ac.uk/pdbsum/4cno PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cno ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AROD_SALTI AROD_SALTI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Structural, biochemical and computational studies to study substrate binding and the role of the conserved residues of the DHQ1 (type I dehydroquinase) enzyme active site are reported in the present paper. The crystal structure of DHQ1 from Salmonella typhi in complex with (2R)-2-methyl-3-dehydroquinic acid, a substrate analogue, was solved at 1.5 A. The present study reveals a previously unknown key role for conserved Glu46, Phe145 and Met205 and Gln236, Pro234 and Ala233 residues, with the latter three being located in the flexible substrate-covering loop. Gln236 was shown to be responsible for the folding of this loop and for the dramatic reduction of its flexibility, which triggers active site closure. Glu46 was found to be key in bringing the substrate close to the lysine/histidine catalytic pocket to initiate catalysis. The present study could be useful in the rational design of inhibitors of this challenging and recognized target for the development of novel herbicides and antimicrobial agents.

Insights into substrate binding and catalysis in bacterial type I dehydroquinase.,Maneiro M, Peon A, Lence E, Otero JM, Van Raaij MJ, Thompson P, Hawkins AR, Gonzalez-Bello C Biochem J. 2014 Sep 15;462(3):415-24. doi: 10.1042/BJ20140614. PMID:24957267<ref>PMID:24957267</ref>

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

==See Also==
*[[Dehydroquinase 3D structures|Dehydroquinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Salmonella enterica subsp. enterica serovar Typhi]]
[[Category: Gonzalez-Bello C]]
[[Category: Hawkins AR]]
[[Category: Lamb H]]
[[Category: Lence E]]
[[Category: Llamas-Saiz AL]]
[[Category: Maneiro M]]
[[Category: Otero JM]]
[[Category: Peon A]]
[[Category: Van Raaij MJ]]