3oic

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<StructureSection load='3oic' size='340' side='right'caption='[[3oic]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3oic' size='340' side='right'caption='[[3oic]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3oic]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OIC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OIC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3oic]] is a 2 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=3OIC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OIC FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3oid|3oid]], [[3oif|3oif]], [[3oig|3oig]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FabL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Enoyl-[acyl-carrier-protein]_reductase_(NADPH,_B-specific) Enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.10 1.3.1.10] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3oic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oic OCA], [https://pdbe.org/3oic PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oic RCSB], [https://www.ebi.ac.uk/pdbsum/3oic PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oic ProSAT]</span></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=3oic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oic OCA], [https://pdbe.org/3oic PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oic RCSB], [https://www.ebi.ac.uk/pdbsum/3oic PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oic ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3oic" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Vibrio subtilis ehrenberg 1835]]
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[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ha, B H]]
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[[Category: Ha BH]]
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[[Category: Hong, S K]]
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[[Category: Hong SK]]
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[[Category: Hwang, K Y]]
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[[Category: Hwang KY]]
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[[Category: Kim, E E]]
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[[Category: Kim EE]]
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[[Category: Kim, K H]]
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[[Category: Kim K-H]]
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[[Category: Kim, S J]]
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[[Category: Kim SJ]]
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[[Category: Enoyl-acp reductase]]
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[[Category: Fabl]]
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[[Category: Fatty acid synthesis]]
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[[Category: Nadph binding]]
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[[Category: Oxidoreductase]]
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[[Category: Rossmann-like fold]]
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Current revision

Crystal Structure of Enoyl-ACP Reductases III (FabL) from B. subtilis (apo form)

PDB ID 3oic

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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