3il5: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3il5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IL5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IL5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3il5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IL5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IL5 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B82:2-({[4-BROMO-3-(DIETHYLSULFAMOYL)PHENYL]CARBONYL}AMINO)BENZOIC+ACID'>B82</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B82:2-({[4-BROMO-3-(DIETHYLSULFAMOYL)PHENYL]CARBONYL}AMINO)BENZOIC+ACID'>B82</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3il3|3il3]], [[3il4|3il4]], [[3il6|3il6]], [[3il7|3il7]], [[3il9|3il9]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3il3|3il3]], [[3il4|3il4]], [[3il6|3il6]], [[3il7|3il7]], [[3il9|3il9]]</td></tr> | ||
<tr><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 faecalis])</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 faecalis])</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_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><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://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://www.rcsb.org/pdb/explore.do?structureId=3il5 RCSB], [http://www.ebi.ac.uk/pdbsum/3il5 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/FABH_ENTFA 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Beta-ketoacyl-acyl-carrier-protein synthase III]] | [[Category: Beta-ketoacyl-acyl-carrier-protein synthase III]] | ||
[[Category: Enterococcus faecalis]] | [[Category: Enterococcus faecalis]] | ||
[[Category: Appelt, K | [[Category: Appelt, K]] | ||
[[Category: Cortez, J | [[Category: Cortez, J]] | ||
[[Category: Gajiwala, K S | [[Category: Gajiwala, K S]] | ||
[[Category: Lu, J | [[Category: Lu, J]] | ||
[[Category: Margosiak, S]] | [[Category: Margosiak, S]] | ||
[[Category: Nie, Z | [[Category: Nie, Z]] | ||
[[Category: Su, Y | [[Category: Su, Y]] | ||
[[Category: Acyltransferase]] | [[Category: Acyltransferase]] | ||
[[Category: Antibiotic]] | [[Category: Antibiotic]] | ||
Revision as of 04:17, 25 December 2014
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. See AlsoReferences
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