View source for 3oid


==Crystal Structure of Enoyl-ACP Reductases III (FabL) from B. subtilis (complex with NADP and TCL)==
<StructureSection load='3oid' size='340' side='right'caption='[[3oid]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3oid]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OID 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=TCL:TRICLOSAN'>TCL</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=3oid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oid OCA], [https://pdbe.org/3oid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oid RCSB], [https://www.ebi.ac.uk/pdbsum/3oid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oid ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FABL_BACSU FABL_BACSU] Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). It confers resistance to triclosan.<ref>PMID:11007778</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enoyl-[acyl carrier protein] (ACP) reductase (ENR) is a key enzyme in type II fatty acid synthesis that catalyzes the last step in each elongation cycle. Therefore, it has been considered as a target for antibiotics. However, recent studies indicate that some pathogens have more than one ENR; in particular, Bacillus subtilis has two ENRs, FabI and FabL. The crystal structures of the ternary complexes of BsFaBI and BsFabL are found as a homotetramer showing the same overall structure despite a sequence identity of only 24%. The positions of the catalytic dyad of Tyr-(Xaa)(6)-Lys in FabL are almost identical to that of FabI, but a detailed structural analysis shows that FabL shares more structural similarities with FabG and other members of the SDR (short-chain alcohol dehydrogenase/reductase) family. The apo FabL structure shows significantly different conformations at the cofactor and the substrate-binding regions, and this resulted in a totally different tetrameric arrangement reflecting the flexibility of these regions in the absence of the cofactor and substrate/inhibitor.

Crystal Structures of Enoyl-ACP Reductases I (FabI) and III (FabL) from B. subtilis.,Kim KH, Ha BH, Kim SJ, Hong SK, Hwang KY, Kim EE J Mol Biol. 2011 Feb 25;406(3):403-15. Epub 2010 Dec 23. PMID:21185310<ref>PMID:21185310</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3oid" style="background-color:#fffaf0;"></div>

==See Also==
*[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Ha BH]]
[[Category: Hong SK]]
[[Category: Hwang KY]]
[[Category: Kim EE]]
[[Category: Kim K-H]]
[[Category: Kim SJ]]