1kas
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1kas. | + | [[Image:1kas.jpg|left|200px]]<br /><applet load="1kas" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1kas" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1kas, resolution 2.4Å" /> | caption="1kas, resolution 2.4Å" /> | ||
'''BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI'''<br /> | '''BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI'''<br /> | ||
| Line 8: | Line 7: | ||
==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/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] | + | 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== | ||
| Line 30: | Line 29: | ||
[[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 Dec 18 16:39:38 2007'' |
Revision as of 14:29, 18 December 2007
|
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
Page seeded by OCA on Tue Dec 18 16:39:38 2007
Categories: Beta-ketoacyl-acyl-carrier-protein synthase I | Escherichia coli | Fatty Acid Synthase | Single protein | Dehesh, K. | Edwards, P. | Huang, W. | Jia, J. | Lindqvist, Y. | Schneider, G. | Acyltransferase | Alpha-beta protein | Alpha-beta-alpha-beta-alpha | Condensing enzyme | Fatty acid elongation | Five-layered fold | Lipid metabolism
