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1g5x

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(New page: 200px<br /><applet load="1g5x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g5x, resolution 2.45&Aring;" /> '''The Structure of Bet...)
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[[Image:1g5x.jpg|left|200px]]<br /><applet load="1g5x" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1g5x, resolution 2.45&Aring;" />
 
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'''The Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase I'''<br />
 
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==Overview==
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==The Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase I==
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The molecular details that govern the specific interactions between acyl, carrier protein (ACP) and the enzymes of fatty acid biosynthesis are, unknown. We investigated the mechanism of ACP-protein interactions using a, computational analysis to dock the NMR structure of ACP with the crystal, structure of beta-ketoacyl-ACP synthase III (FabH) and experimentally, tested the model by the biochemical analysis of FabH mutants. The, activities of the mutants were assessed using both an ACP-dependent and an, ACP-independent assay. The ACP interaction surface was defined by, mutations that compromised FabH activity in the ACP-dependent assay but, had no effect in the ACP-independent assay. ACP docked to a positively, charged/hydrophobic patch adjacent to the active site tunnel on FabH, which included a conserved arginine (Arg-249) that was required for ACP, docking. Kinetic analysis and direct binding studies between FabH and ACP, confirmed the identification of Arg-249 as critical for FabH-ACP, interaction. Our experiments reveal the significance of the positively, charged/hydrophobic patch located adjacent to the active site cavities of, the fatty acid biosynthesis enzymes and the high degree of sequence, conservation in helix II of ACP across species.
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<StructureSection load='1g5x' size='340' side='right'caption='[[1g5x]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1g5x]] 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=1G5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G5X 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]] 2.45&#8491;</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=1g5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g5x OCA], [https://pdbe.org/1g5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g5x RCSB], [https://www.ebi.ac.uk/pdbsum/1g5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g5x 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/g5/1g5x_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=1g5x ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1G5X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G5X OCA].
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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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==Reference==
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</StructureSection>
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Identification and analysis of the acyl carrier protein (ACP) docking site on beta-ketoacyl-ACP synthase III., Zhang YM, Rao MS, Heath RJ, Price AC, Olson AJ, Rock CO, White SW, J Biol Chem. 2001 Mar 16;276(11):8231-8. Epub 2000 Nov 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11078736 11078736]
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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: Heath, R.J.]]
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[[Category: Heath RJ]]
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[[Category: Olson, A.J.]]
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[[Category: Olson AJ]]
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[[Category: Price, A.C.]]
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[[Category: Price AC]]
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[[Category: Rao, M.S.]]
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[[Category: Rao MS]]
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[[Category: Rock, C.O.]]
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[[Category: Rock CO]]
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[[Category: White, S.W.]]
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[[Category: White SW]]
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[[Category: Zhang, Y.M.]]
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[[Category: Zhang YM]]
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[[Category: enzyme]]
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[[Category: gene duplication]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:44:06 2007''
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Current revision

The Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase I

PDB ID 1g5x

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