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1kas

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[[Image:1kas.gif|left|200px]]<br />
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[[Image:1kas.jpg|left|200px]]<br /><applet load="1kas" size="450" color="white" frame="true" align="right" spinBox="true"
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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;" />
caption="1kas, resolution 2.4&Aring;" />
'''BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI'''<br />
'''BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI'''<br />
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==About this Structure==
==About this Structure==
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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/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].
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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/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] Known structural/functional Site: <scene name='pdbsite=ACT:Active Site Residue'>ACT</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KAS OCA].
==Reference==
==Reference==
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[[Category: lipid metabolism]]
[[Category: lipid metabolism]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:41:07 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:39:38 2007''

Revision as of 14:29, 18 December 2007


1kas, resolution 2.4Å

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BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI

Overview

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.

About this Structure

1KAS is a Single protein structure of sequence from Escherichia coli. The following page contains interesting information on the relation of 1KAS with [Fatty Acid Synthase]. Active as Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

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

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