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| | <StructureSection load='3oid' size='340' side='right'caption='[[3oid]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='3oid' size='340' side='right'caption='[[3oid]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3oid]] is a 4 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=3OID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OID FirstGlance]. <br> | + | <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='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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3oic|3oic]], [[3oif|3oif]], [[3oig|3oig]]</div></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='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> | + | |
| - | <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>
| + | |
| | <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> | | <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> | | </table> |
| | == Function == | | == 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>
| + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ha, B H]] | + | [[Category: Ha BH]] |
| - | [[Category: Hong, S K]] | + | [[Category: Hong SK]] |
| - | [[Category: Hwang, K Y]] | + | [[Category: Hwang KY]] |
| - | [[Category: Kim, E E]] | + | [[Category: Kim EE]] |
| - | [[Category: Kim, K H]] | + | [[Category: Kim K-H]] |
| - | [[Category: Kim, S J]] | + | [[Category: Kim SJ]] |
| - | [[Category: Enoyl-acp reductase]]
| + | |
| - | [[Category: Fabl]]
| + | |
| - | [[Category: Fatty acid synthesis]]
| + | |
| - | [[Category: Nadph binding]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Rossmann-like fold]]
| + | |
| Structural highlights
Function
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Heath RJ, Su N, Murphy CK, Rock CO. The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis. J Biol Chem. 2000 Dec 22;275(51):40128-33. PMID:11007778 doi:http://dx.doi.org/10.1074/jbc.M005611200
- ↑ Kim KH, Ha BH, Kim SJ, Hong SK, Hwang KY, Kim EE. Crystal Structures of Enoyl-ACP Reductases I (FabI) and III (FabL) from B. subtilis. J Mol Biol. 2011 Feb 25;406(3):403-15. Epub 2010 Dec 23. PMID:21185310 doi:10.1016/j.jmb.2010.12.003
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