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[[Image:1kas.gif|left|200px]]<br />
<applet load="1kas" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1kas, resolution 2.4&Aring;" />
'''BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI'''<br />


==Overview==
==BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI==
In the biosynthesis of fatty acids, the beta-ketoacyl-acyl carrier protein, (ACP) synthases catalyze chain elongation by the addition of two-carbon, units derived from malonyl-ACP to an acyl group bound to either ACP or, CoA. The crystal structure of beta-ketoacyl synthase II from Escherichia, coli has been determined with the multiple isomorphous replacement method, and refined at 2.4 A resolution. The subunit consists of two mixed, five-stranded beta-sheets surrounded by alpha-helices. The two sheets are, packed against each other in such a way that the fold can be described as, consisting of five layers, alpha-beta-alpha-beta-alpha. The enzyme is a, homodimer, and the subunits are related by a crystallographic 2-fold axis., The two active sites are located near the dimer interface but are, approximately 25 A apart. The proposed nucleophile in the reaction, Cys163, is located at the bottom of a mainly hydrophobic pocket which is, also lined with several conserved polar residues. In spite of very low, overall sequence homology, the structure of beta-ketoacyl synthase is, similar to that of thiolase, an enzyme involved in the beta-oxidation, pathway, indicating that both enzymes might have a common ancestor.
<StructureSection load='1kas' size='340' side='right'caption='[[1kas]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1kas]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The June 2007 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Fatty Acid Synthase''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2007_6 10.2210/rcsb_pdb/mom_2007_6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KAS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kas OCA], [https://pdbe.org/1kas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kas RCSB], [https://www.ebi.ac.uk/pdbsum/1kas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kas ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FABF_ECOLI FABF_ECOLI] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ka/1kas_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1kas ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1KAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 1KAS with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb90_1.html Fatty Acid Synthase]]. 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] Structure known Active Site: ACT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KAS OCA].
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes., Huang W, Jia J, Edwards P, Dehesh K, Schneider G, Lindqvist Y, EMBO J. 1998 Mar 2;17(5):1183-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9482715 9482715]
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Fatty Acid Synthase]]
[[Category: Fatty Acid Synthase]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Dehesh, K.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Edwards, P.]]
[[Category: Dehesh K]]
[[Category: Huang, W.]]
[[Category: Edwards P]]
[[Category: Jia, J.]]
[[Category: Huang W]]
[[Category: Lindqvist, Y.]]
[[Category: Jia J]]
[[Category: Schneider, G.]]
[[Category: Lindqvist Y]]
[[Category: acyltransferase]]
[[Category: Schneider G]]
[[Category: alpha-beta protein]]
[[Category: alpha-beta-alpha-beta-alpha]]
[[Category: condensing enzyme]]
[[Category: fatty acid elongation]]
[[Category: five-layered fold]]
[[Category: lipid metabolism]]
 
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Retrieved from "https://proteopedia.org/1kas"