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1kas

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[[Image:1kas.gif|left|200px]]<br />
 
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<applet load="1kas" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1kas, resolution 2.4&Aring;" />
 
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'''BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI'''<br />
 
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==Overview==
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==BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI==
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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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9482715 (full description)]]
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<StructureSection load='1kas' size='340' side='right'caption='[[1kas]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<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>
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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]] 2.4&#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=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>
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</table>
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== Function ==
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[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.
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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/ka/1kas_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=1kas 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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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/Transferase Transferase]], 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]].
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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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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]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Fatty Acid Synthase]]
[[Category: Fatty Acid Synthase]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Dehesh, K.]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Edwards, P.]]
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[[Category: Dehesh K]]
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[[Category: Huang, W.]]
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[[Category: Edwards P]]
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[[Category: Jia, J.]]
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[[Category: Huang W]]
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[[Category: Lindqvist, Y.]]
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[[Category: Jia J]]
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[[Category: Schneider, G.]]
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[[Category: Lindqvist Y]]
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[[Category: acyltransferase]]
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[[Category: Schneider G]]
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[[Category: alpha-beta protein]]
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[[Category: alpha-beta-alpha-beta-alpha]]
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[[Category: condensing enzyme]]
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[[Category: fatty acid elongation]]
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[[Category: five-layered fold]]
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[[Category: lipid metabolism]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:29:52 2007''
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Current revision

BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI

PDB ID 1kas

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