2vb8: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2vb8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VB8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VB8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2vb8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VB8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VB8 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TLM:THIOLACTOMYCIN'>TLM</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TLM:THIOLACTOMYCIN'>TLM</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f91|1f91]], [[1fj8|1fj8]], [[1g5x|1g5x]], [[1h4f|1h4f]], [[2aq7|2aq7]], [[2aqb|2aqb]], [[2buh|2buh]], [[2bui|2bui]], [[2byx|2byx]], [[2bz3|2bz3]], [[1dd8|1dd8]], [[1ek4|1ek4]], [[1fj4|1fj4]], [[2byw|2byw]], [[2byy|2byy]], [[2byz|2byz]], [[2bz4|2bz4]], [[2vb7|2vb7]], [[2vb9|2vb9]], [[2vba|2vba]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f91|1f91]], [[1fj8|1fj8]], [[1g5x|1g5x]], [[1h4f|1h4f]], [[2aq7|2aq7]], [[2aqb|2aqb]], [[2buh|2buh]], [[2bui|2bui]], [[2byx|2byx]], [[2bz3|2bz3]], [[1dd8|1dd8]], [[1ek4|1ek4]], [[1fj4|1fj4]], [[2byw|2byw]], [[2byy|2byy]], [[2byz|2byz]], [[2bz4|2bz4]], [[2vb7|2vb7]], [[2vb9|2vb9]], [[2vba|2vba]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-acyl-carrier-protein_synthase_I Beta-ketoacyl-acyl-carrier-protein synthase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-acyl-carrier-protein_synthase_I Beta-ketoacyl-acyl-carrier-protein synthase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vb8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vb8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vb8 PDBsum]</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=2vb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vb8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vb8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vb8 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/FABB_ECOLI FABB_ECOLI]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 35: | Line 37: | ||
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]] | [[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Bailly, J | [[Category: Bailly, J]] | ||
[[Category: Hennig, M | [[Category: Hennig, M]] | ||
[[Category: Pappenberger, G | [[Category: Pappenberger, G]] | ||
[[Category: Schulz-Gasch, T | [[Category: Schulz-Gasch, T]] | ||
[[Category: Acyltransferase]] | [[Category: Acyltransferase]] | ||
[[Category: Antibiotic]] | [[Category: Antibiotic]] | ||
Revision as of 14:18, 25 December 2014
BETA-KETOACYL-ACP SYNTHASE I (KAS) FROM E. COLI WITH BOUND INHIBITOR THIOLACTOMYCINBETA-KETOACYL-ACP SYNTHASE I (KAS) FROM E. COLI WITH BOUND INHIBITOR THIOLACTOMYCIN
Structural highlights
Function[FABB_ECOLI] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedFatty-acid synthesis in bacteria is of great interest as a target for the discovery of antibacterial compounds. The addition of a new acetyl moiety to the growing fatty-acid chain, an essential step in this process, is catalyzed by beta-ketoacyl-ACP synthase (KAS). It is inhibited by natural antibiotics such as cerulenin and thiolactomycin; however, these lack the requirements for optimal drug development. Structure-based biophysical screening revealed a novel synthetic small molecule, 2-phenylamino-4-methyl-5-acetylthiazole, that binds to Escherichia coli KAS I with a binding constant of 25 microM as determined by fluorescence titration. A 1.35 A crystal structure of its complex with its target reveals noncovalent interactions with the active-site Cys163 and hydrophobic residues of the fatty-acid binding pocket. The active site is accessible through an open conformation of the Phe392 side chain and no conformational changes are induced at the active site upon ligand binding. This represents a novel binding mode that differs from thiolactomycin or cerulenin interaction. The structural information on the protein-ligand interaction offers strategies for further optimization of this low-molecular-weight compound. Structure-assisted discovery of an aminothiazole derivative as a lead molecule for inhibition of bacterial fatty-acid synthesis.,Pappenberger G, Schulz-Gasch T, Kusznir E, Muller F, Hennig M Acta Crystallogr D Biol Crystallogr. 2007 Dec;63(Pt 12):1208-16. Epub 2007, Nov 16. PMID:18084068[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||