1kas
From Proteopedia
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|SITE= <scene name='pdbsite=ACT:Active+Site+Residue'>ACT</scene> | |SITE= <scene name='pdbsite=ACT:Active+Site+Residue'>ACT</scene> | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [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] | + | |ACTIVITY= <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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<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://www.ebi.ac.uk/pdbsum/1kas PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kas RCSB]</span> | ||
}} | }} | ||
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[[Category: lipid metabolism]] | [[Category: lipid metabolism]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:45:49 2008'' |
Revision as of 18:45, 30 March 2008
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| , resolution 2.4Å | |||||||
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| Sites: | |||||||
| Activity: | Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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]. 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 Sun Mar 30 21:45:49 2008
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
