3il5: Difference between revisions
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==Structure of E. faecalis FabH in complex with 2-({4-bromo-3-[(diethylamino)sulfonyl]benzoyl}amino)benzoic acid== | ==Structure of E. faecalis FabH in complex with 2-({4-bromo-3-[(diethylamino)sulfonyl]benzoyl}amino)benzoic acid== | ||
<StructureSection load='3il5' size='340' side='right' caption='[[3il5]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='3il5' size='340' side='right' caption='[[3il5]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EF_2885, fabH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1351 "Enterococcus proteiformis" Thiercelin and Jouhaud 1903])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EF_2885, fabH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1351 "Enterococcus proteiformis" Thiercelin and Jouhaud 1903])</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_III Beta-ketoacyl-[acyl-carrier-protein] synthase III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.180 2.3.1.180] </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_III Beta-ketoacyl-[acyl-carrier-protein] synthase III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.180 2.3.1.180] </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=3il5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3il5 OCA], [http://pdbe.org/3il5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3il5 RCSB], [http://www.ebi.ac.uk/pdbsum/3il5 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=3il5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3il5 OCA], [http://pdbe.org/3il5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3il5 RCSB], [http://www.ebi.ac.uk/pdbsum/3il5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3il5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/il/3il5_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/il/3il5_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 3il5" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3il5" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Acyltransferase]] | [[Category: Acyltransferase]] | ||
[[Category: Antibiotic]] | [[Category: Antibiotic]] | ||
[[Category: Cytoplasm]] | |||
[[Category: Fabh]] | [[Category: Fabh]] | ||
[[Category: Fatty acid biosynthesis]] | [[Category: Fatty acid biosynthesis]] | ||
Revision as of 22:21, 24 January 2018
Structure of E. faecalis FabH in complex with 2-({4-bromo-3-[(diethylamino)sulfonyl]benzoyl}amino)benzoic acidStructure of E. faecalis FabH in complex with 2-({4-bromo-3-[(diethylamino)sulfonyl]benzoyl}amino)benzoic acid
Structural highlights
Function[FABH_ENTFA] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity). 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 PubMedFabH (beta-ketoacyl-acyl carrier protein synthase III) is unique in that it initiates fatty acid biosynthesis, is inhibited by long-chain fatty acids providing means for feedback control of the process, and dictates the fatty acid profile of the organism by virtue of its substrate specificity. We report the crystal structures of bacterial FabH enzymes from four different pathogenic species: Enterococcus faecalis, Haemophilus influenzae, Staphylococcus aureus and Escherichia coli. Structural data on the enzyme from different species show important differences in the architecture of the substrate-binding sites that parallel the inter-species diversity in the substrate specificities of these enzymes. Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme.,Gajiwala KS, Margosiak S, Lu J, Cortez J, Su Y, Nie Z, Appelt K FEBS Lett. 2009 Sep 3;583(17):2939-46. Epub 2009 Aug 6. PMID:19665020[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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