1kas: Difference between revisions

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 <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 [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. The June 2007 RCSB PDB [http://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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KAS FirstGlance]. <br>
+<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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
+</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kas OCA], [http://pdbe.org/1kas PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kas RCSB], [http://www.ebi.ac.uk/pdbsum/1kas PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kas ProSAT]</span></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 ==
-[[http://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.
+[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]]
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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].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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:9482715<ref>PMID:9482715</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1kas" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Fatty Acid Synthase]]
 [[Category: Large Structures]]
 [[Category: RCSB PDB Molecule of the Month]]
-[[Category: Dehesh, K]]
+[[Category: Dehesh K]]
-[[Category: Edwards, P]]
+[[Category: Edwards P]]
-[[Category: Huang, W]]
+[[Category: Huang W]]
-[[Category: Jia, J]]
+[[Category: Jia J]]
-[[Category: Lindqvist, Y]]
+[[Category: Lindqvist Y]]
-[[Category: Schneider, G]]
+[[Category: Schneider G]]
-[[Category: Acyltransferase]]
-[[Category: Alpha-beta protein]]
-[[Category: Alpha-beta-alpha-beta-alpha]]
-[[Category: Condensing enzyme]]
-[[Category: Fatty acid elongation]]
-[[Category: Five-layered fold]]
-[[Category: Lipid metabolism]]