This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3oid
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | [[ | + | ==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]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3oid]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OID FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=TCL:TRICLOSAN'>TCL</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3oic|3oic]], [[3oif|3oif]], [[3oig|3oig]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FabL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Enoyl-[acyl-carrier-protein]_reductase_(NADPH,_B-specific) Enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific)], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3oid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oid OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oid RCSB], [http://www.ebi.ac.uk/pdbsum/3oid PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
==See Also== | ==See Also== | ||
*[[Enoyl-Acyl-Carrier Protein Reductase|Enoyl-Acyl-Carrier Protein Reductase]] | *[[Enoyl-Acyl-Carrier Protein Reductase|Enoyl-Acyl-Carrier Protein Reductase]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
| - | [[Category: Ha, B H | + | [[Category: Ha, B H]] |
| - | [[Category: Hong, S K | + | [[Category: Hong, S K]] |
| - | [[Category: Hwang, K Y | + | [[Category: Hwang, K Y]] |
| - | [[Category: Kim, E E | + | [[Category: Kim, E E]] |
| - | [[Category: Kim, K H | + | [[Category: Kim, K H]] |
| - | [[Category: Kim, S J | + | [[Category: Kim, S J]] |
[[Category: Enoyl-acp reductase]] | [[Category: Enoyl-acp reductase]] | ||
[[Category: Fabl]] | [[Category: Fabl]] | ||
Revision as of 13:11, 9 December 2014
Crystal Structure of Enoyl-ACP Reductases III (FabL) from B. subtilis (complex with NADP and TCL)
| |||||||||||
