1h4f

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(New page: 200px<br /> <applet load="1h4f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h4f, resolution 2.00&Aring;" /> '''E. COLI BETA-KETOAC...)
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[[Image:1h4f.gif|left|200px]]<br />
 
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<applet load="1h4f" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1h4f, resolution 2.00&Aring;" />
 
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'''E. COLI BETA-KETOACYL [ACYL CARRIER PROTEIN] SYNTHASE I K328R'''<br />
 
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==Overview==
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==E. COLI BETA-KETOACYL [ACYL CARRIER PROTEIN] SYNTHASE I K328R==
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Beta-ketoacyl-acyl carrier protein (ACP) synthase enzymes join short, carbon units to construct fatty acyl chains by a three-step Claisen, condensation reaction. The reaction starts with a trans thioesterification, of the acyl primer substrate from ACP to the enzyme. Subsequently, the, donor substrate malonyl-ACP is decarboxylated to form a carbanion, intermediate, which in the third step attacks C1 of the primer substrate, giving rise to an elongated acyl chain. A subgroup of beta-ketoacyl-ACP, synthases, including mitochondrial beta-ketoacyl-ACP synthase, bacterial, plus plastid beta-ketoacyl-ACP synthases I and II, and a domain of human, fatty acid synthase, have a Cys-His-His triad and also a completely, conserved Lys in the active site. To examine the role of these residues in, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?16441657 (full description)]]
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<StructureSection load='1h4f' size='340' side='right'caption='[[1h4f]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1h4f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H4F FirstGlance]. <br>
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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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene></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=1h4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4f OCA], [https://pdbe.org/1h4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h4f RCSB], [https://www.ebi.ac.uk/pdbsum/1h4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h4f ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://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.
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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/h4/1h4f_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=1h4f ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Beta-ketoacyl-acyl carrier protein (ACP) synthase enzymes join short carbon units to construct fatty acyl chains by a three-step Claisen condensation reaction. The reaction starts with a trans thioesterification of the acyl primer substrate from ACP to the enzyme. Subsequently, the donor substrate malonyl-ACP is decarboxylated to form a carbanion intermediate, which in the third step attacks C1 of the primer substrate giving rise to an elongated acyl chain. A subgroup of beta-ketoacyl-ACP synthases, including mitochondrial beta-ketoacyl-ACP synthase, bacterial plus plastid beta-ketoacyl-ACP synthases I and II, and a domain of human fatty acid synthase, have a Cys-His-His triad and also a completely conserved Lys in the active site. To examine the role of these residues in catalysis, H298Q, H298E and six K328 mutants of Escherichia colibeta-ketoacyl-ACP synthase I were constructed and their ability to carry out the trans thioesterification, decarboxylation and/or condensation steps of the reaction was ascertained. The crystal structures of wild-type and eight mutant enzymes with and/or without bound substrate were determined. The H298E enzyme shows residual decarboxylase activity in the pH range 6-8, whereas the H298Q enzyme appears to be completely decarboxylation deficient, showing that H298 serves as a catalytic base in the decarboxylation step. Lys328 has a dual role in catalysis: its charge influences acyl transfer to the active site Cys, and the steric restraint imposed on H333 is of critical importance for decarboxylation activity. This restraint makes H333 an obligate hydrogen bond donor at Nepsilon, directed only towards the active site and malonyl-ACP binding area in the fatty acid complex.
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==About this Structure==
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Fatty acid synthesis. Role of active site histidines and lysine in Cys-His-His-type beta-ketoacyl-acyl carrier protein synthases.,von Wettstein-Knowles P, Olsen JG, McGuire KA, Henriksen A FEBS J. 2006 Feb;273(4):695-710. PMID:16441657<ref>PMID:16441657</ref>
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1H4F is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with NH4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H4F OCA]].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Fatty acid synthesis. Role of active site histidines and lysine in Cys-His-His-type beta-ketoacyl-acyl carrier protein synthases., von Wettstein-Knowles P, Olsen JG, McGuire KA, Henriksen A, FEBS J. 2006 Feb;273(4):695-710. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16441657 16441657]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 1h4f" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Henriksen, A.]]
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[[Category: Mcguire, K.]]
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[[Category: Olsen, J.G.]]
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[[Category: Wettstein-Knowles, P.V.]]
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[[Category: NH4]]
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[[Category: claisen condensation]]
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[[Category: fatty acid synthase]]
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[[Category: thiolase fold]]
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[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 19:37:12 2007''
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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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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Henriksen A]]
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[[Category: Mcguire KA]]
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[[Category: Olsen JG]]
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[[Category: Von Wettstein-Knowles P]]

Current revision

E. COLI BETA-KETOACYL [ACYL CARRIER PROTEIN] SYNTHASE I K328R

PDB ID 1h4f

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