1b3n

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[[Image:1b3n.gif|left|200px]]
[[Image:1b3n.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1b3n |SIZE=350|CAPTION= <scene name='initialview01'>1b3n</scene>, resolution 2.65&Aring;
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The line below this paragraph, containing "STRUCTURE_1b3n", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CER:(2S,+3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE'>CER</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE= FABF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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-->
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|DOMAIN=
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{{STRUCTURE_1b3n| PDB=1b3n | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b3n OCA], [http://www.ebi.ac.uk/pdbsum/1b3n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b3n RCSB]</span>
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}}
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'''BETA-KETOACYL CARRIER PROTEIN SYNTHASE AS A DRUG TARGET, IMPLICATIONS FROM THE CRYSTAL STRUCTURE OF A COMPLEX WITH THE INHIBITOR CERULENIN.'''
'''BETA-KETOACYL CARRIER PROTEIN SYNTHASE AS A DRUG TARGET, IMPLICATIONS FROM THE CRYSTAL STRUCTURE OF A COMPLEX WITH THE INHIBITOR CERULENIN.'''
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[[Category: Moche, M.]]
[[Category: Moche, M.]]
[[Category: Schneider, G.]]
[[Category: Schneider, G.]]
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[[Category: cerulenin inhibition]]
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[[Category: Cerulenin inhibition]]
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[[Category: condensing enzyme]]
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[[Category: Condensing enzyme]]
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[[Category: drug design]]
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[[Category: Drug design]]
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[[Category: drug target]]
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[[Category: Drug target]]
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[[Category: fatty acid elongation]]
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[[Category: Fatty acid elongation]]
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[[Category: lipid metabolism]]
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[[Category: Lipid metabolism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:01:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:52:52 2008''
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Revision as of 08:01, 2 May 2008

Image:1b3n.gif

Template:STRUCTURE 1b3n

BETA-KETOACYL CARRIER PROTEIN SYNTHASE AS A DRUG TARGET, IMPLICATIONS FROM THE CRYSTAL STRUCTURE OF A COMPLEX WITH THE INHIBITOR CERULENIN.


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 enzyme is a possible drug target for treatment of certain cancers and for tuberculosis. The crystal structure of the complex of the enzyme from Escherichia coli, and the fungal mycotoxin cerulenin reveals that the inhibitor is bound in a hydrophobic pocket formed at the dimer interface. Cerulenin is covalently attached to the active site cysteine through its C2 carbon atom. The fit of the inhibitor to the active site is not optimal, and there is thus room for improvement through structure based design.

About this Structure

1B3N is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of the complex between the antibiotic cerulenin and its target, beta-ketoacyl-acyl carrier protein synthase., Moche M, Schneider G, Edwards P, Dehesh K, Lindqvist Y, J Biol Chem. 1999 Mar 5;274(10):6031-4. PMID:10037680 Page seeded by OCA on Fri May 2 11:01:24 2008

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