4z8d

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<StructureSection load='4z8d' size='340' side='right'caption='[[4z8d]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='4z8d' size='340' side='right'caption='[[4z8d]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4z8d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z8D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z8D FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4z8d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z8D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z8D FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4LB:TRANS-4-[({[(2-CHLOROBENZYL)OXY]CARBONYL}AMINO)METHYL]CYCLOHEXANECARBOXYLIC+ACID'>4LB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabH, Z1730, ECs1469 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4LB:TRANS-4-[({[(2-CHLOROBENZYL)OXY]CARBONYL}AMINO)METHYL]CYCLOHEXANECARBOXYLIC+ACID'>4LB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4z8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z8d OCA], [https://pdbe.org/4z8d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z8d RCSB], [https://www.ebi.ac.uk/pdbsum/4z8d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z8d ProSAT]</span></td></tr>
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<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=4z8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z8d OCA], [http://pdbe.org/4z8d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z8d RCSB], [http://www.ebi.ac.uk/pdbsum/4z8d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4z8d ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/FABH_ECO57 FABH_ECO57]] 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.[HAMAP-Rule:MF_01815]
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[https://www.uniprot.org/uniprot/FABH_ECOLI FABH_ECOLI] 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. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain.[HAMAP-Rule:MF_01815]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Fatty acid biosynthesis is essential to bacterial growth in Gram-negative pathogens. Several small molecules identified through a combination of high-throughput and fragment screening were cocrystallized with FabH (beta-ketoacyl-acyl carrier protein synthase III) from Escherichia coli and Streptococcus pneumoniae. Structure-based drug design was used to merge several scaffolds to provide a new class of inhibitors. After optimization for Gram-negative enzyme inhibitory potency, several compounds demonstrated antimicrobial activity against an efflux-negative strain of Haemophilus influenzae. Mutants resistant to these compounds had mutations in the FabH gene near the catalytic triad, validating FabH as a target for antimicrobial drug discovery.
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Antibacterial FabH Inhibitors with Mode of Action Validated in Haemophilus influenzae by in Vitro Resistance Mutation Mapping.,McKinney DC, Eyermann CJ, Gu RF, Hu J, Kazmirski SL, Lahiri SD, McKenzie AR, Shapiro AB, Breault G ACS Infect Dis. 2016 Jul 8;2(7):456-64. doi: 10.1021/acsinfecdis.6b00053. Epub, 2016 May 9. PMID:27626097<ref>PMID:27626097</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4z8d" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Eco57]]
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[[Category: Escherichia coli O157:H7]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lahiri, S D]]
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[[Category: Lahiri SD]]
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[[Category: Carbamate]]
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[[Category: Fatty acid biosynthesis]]
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[[Category: Structure based drug design]]
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[[Category: Transferase-transferase inhibitor complex]]
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Current revision

Antibacterial FabH Inhibitors with Validated Mode of Action in Haemophilus Influenzae by in vitro resistance mutation mapping

PDB ID 4z8d

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