View source for 3zu4


==Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH and the 2-pyridone inhibitor PT172==
<StructureSection load='3zu4' size='340' side='right'caption='[[3zu4]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zu4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis_CO92 Yersinia pestis CO92]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZU4 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]] 2.01&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>, <scene name='pdbligand=ZU4:1-(2-CHLOROBENZYL)-4-HEXYLPYRIDIN-2(1H)-ONE'>ZU4</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=3zu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zu4 OCA], [https://pdbe.org/3zu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zu4 RCSB], [https://www.ebi.ac.uk/pdbsum/3zu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zu4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FABV_YERPE FABV_YERPE] Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP).<ref>PMID:22244758</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The recently discovered FabV enoyl-ACP reductase, which catalyzes the last step of the bacterial fatty acid biosynthesis (FAS-II) pathway, is a promising but unexploited drug target against the reemerging pathogen Yersinia pestis. The structure of Y. pestis FabV in complex with its cofactor reveals that the enzyme features the common architecture of the short-chain dehydrogenase reductase superfamily, but contains additional structural elements that are mostly folded around the usually flexible substrate-binding loop, thereby stabilizing it in a very tight conformation that seals the active site. The structures of FabV in complex with NADH and two newly developed 2-pyridone inhibitors provide insights for the development of new lead compounds, and suggest a mechanism by which the substrate-binding loop opens to admit the inhibitor, a motion that could also be coupled to the interaction of FabV with the acyl-carrier protein substrate.

Structure of the Yersinia pestis FabV enoyl-ACP reductase and its interaction with two 2-pyridone inhibitors.,Hirschbeck MW, Kuper J, Lu H, Liu N, Neckles C, Shah S, Wagner S, Sotriffer CA, Tonge PJ, Kisker C Structure. 2012 Jan 11;20(1):89-100. PMID:22244758<ref>PMID:22244758</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zu4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Yersinia pestis CO92]]
[[Category: Hirschbeck MW]]
[[Category: Kisker C]]
[[Category: Kuper J]]
[[Category: Tonge PJ]]