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1hn9

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[[Image:1hn9.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III==
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|PDB= 1hn9 |SIZE=350|CAPTION= <scene name='initialview01'>1hn9</scene>, resolution 2.&Aring;
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<StructureSection load='1hn9' size='340' side='right'caption='[[1hn9]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene>
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<table><tr><td colspan='2'>[[1hn9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1d9b 1d9b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HN9 FirstGlance]. <br>
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|ACTIVITY= [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]
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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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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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}}
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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=1hn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn9 OCA], [https://pdbe.org/1hn9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hn9 RCSB], [https://www.ebi.ac.uk/pdbsum/1hn9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hn9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hn/1hn9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hn9 ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III'''
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==See Also==
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*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Beta-ketoacyl-acyl carrier protein synthase III (FabH), the most divergent member of the family of condensing enzymes, is a key catalyst in bacterial fatty acid biosynthesis and a promising target for novel antibiotics. We report here the crystal structures of FabH determined in the presence and absence of acetyl-CoA. These structures display a fold that is common for condensing enzymes. The observed acetylation of Cys(112) proves its catalytic role and clearly defines the primer binding pocket. Modeling based on a bound CoA molecule suggests catalytic roles for His(244) and Asn(274). The structures provide the molecular basis for FabH substrate specificity and reaction mechanism and are important for structure-based design of novel antibiotics.
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==About this Structure==
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1HN9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry 1D9B. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN9 OCA].
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==Reference==
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Crystal structure of beta-ketoacyl-acyl carrier protein synthase III. A key condensing enzyme in bacterial fatty acid biosynthesis., Qiu X, Janson CA, Konstantinidis AK, Nwagwu S, Silverman C, Smith WW, Khandekar S, Lonsdale J, Abdel-Meguid SS, J Biol Chem. 1999 Dec 17;274(51):36465-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10593943 10593943]
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[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Abdel-Meguid, S S.]]
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[[Category: Abdel-Meguid SS]]
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[[Category: Janson, C A.]]
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[[Category: Janson CA]]
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[[Category: Khandekar, S K.]]
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[[Category: Khandekar SK]]
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[[Category: Konstantinidis, A K.]]
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[[Category: Konstantinidis AK]]
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[[Category: Lonsdale, J.]]
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[[Category: Lonsdale J]]
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[[Category: Nwagwu, S.]]
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[[Category: Nwagwu S]]
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[[Category: Qiu, X.]]
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[[Category: Qiu X]]
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[[Category: Silverman, C.]]
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[[Category: Silverman C]]
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[[Category: Smith, W W.]]
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[[Category: Smith WW]]
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[[Category: PO4]]
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[[Category: fabh]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:39:13 2008''
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Current revision

CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III

PDB ID 1hn9

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