1kas: Difference between revisions
New page: left|200px<br /> <applet load="1kas" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kas, resolution 2.4Å" /> '''BETA-KETOACYL-ACP SY... |
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==About this Structure== | ==About this Structure== | ||
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/ ]], 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=1KAS OCA]]. | 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]]. | ||
==Reference== | ==Reference== | ||
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[[Category: lipid metabolism]] | [[Category: lipid metabolism]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:29:52 2007'' | ||
Revision as of 09:25, 30 October 2007
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BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI
OverviewOverview
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 ... [(full description)]
About this StructureAbout 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 [Transferase], with EC number [2.3.1.41]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
ReferenceReference
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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