2vba

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[[Image:2vba.jpg|left|200px]]<br /><applet load="2vba" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2vba.jpg|left|200px]]
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caption="2vba, resolution 1.36&Aring;" />
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'''BETA-KETOACYL-ACP SYNTHASE I (KAS) FROM E. COLI WITH BOUND AMINO-THIAZOLE INHIBITOR'''<br />
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{{Structure
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|PDB= 2vba |SIZE=350|CAPTION= <scene name='initialview01'>2vba</scene>, resolution 1.36&Aring;
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|SITE= <scene name='pdbsite=AC1:P4t+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=P4T:'>P4T</scene>
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|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]
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|GENE=
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}}
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'''BETA-KETOACYL-ACP SYNTHASE I (KAS) FROM E. COLI WITH BOUND AMINO-THIAZOLE INHIBITOR'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2VBA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=P4T:'>P4T</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=AC1:P4t+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VBA OCA].
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2VBA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VBA OCA].
==Reference==
==Reference==
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Structure-assisted discovery of an aminothiazole derivative as a lead molecule for inhibition of bacterial fatty-acid synthesis., Pappenberger G, Schulz-Gasch T, Kusznir E, Muller F, Hennig M, Acta Crystallogr D Biol Crystallogr. 2007 Dec;63(Pt 12):1208-16. Epub 2007, Nov 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18084068 18084068]
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Structure-assisted discovery of an aminothiazole derivative as a lead molecule for inhibition of bacterial fatty-acid synthesis., Pappenberger G, Schulz-Gasch T, Kusznir E, Muller F, Hennig M, Acta Crystallogr D Biol Crystallogr. 2007 Dec;63(Pt 12):1208-16. Epub 2007, Nov 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18084068 18084068]
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:54:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:45:08 2008''

Revision as of 16:45, 20 March 2008

Image:2vba.jpg


PDB ID 2vba

Drag the structure with the mouse to rotate
, resolution 1.36Å
Sites:
Ligands:
Activity: Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41
Coordinates: save as pdb, mmCIF, xml



BETA-KETOACYL-ACP SYNTHASE I (KAS) FROM E. COLI WITH BOUND AMINO-THIAZOLE INHIBITOR


Overview

Fatty-acid synthesis in bacteria is of great interest as a target for the discovery of antibacterial compounds. The addition of a new acetyl moiety to the growing fatty-acid chain, an essential step in this process, is catalyzed by beta-ketoacyl-ACP synthase (KAS). It is inhibited by natural antibiotics such as cerulenin and thiolactomycin; however, these lack the requirements for optimal drug development. Structure-based biophysical screening revealed a novel synthetic small molecule, 2-phenylamino-4-methyl-5-acetylthiazole, that binds to Escherichia coli KAS I with a binding constant of 25 microM as determined by fluorescence titration. A 1.35 A crystal structure of its complex with its target reveals noncovalent interactions with the active-site Cys163 and hydrophobic residues of the fatty-acid binding pocket. The active site is accessible through an open conformation of the Phe392 side chain and no conformational changes are induced at the active site upon ligand binding. This represents a novel binding mode that differs from thiolactomycin or cerulenin interaction. The structural information on the protein-ligand interaction offers strategies for further optimization of this low-molecular-weight compound.

About this Structure

2VBA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure-assisted discovery of an aminothiazole derivative as a lead molecule for inhibition of bacterial fatty-acid synthesis., Pappenberger G, Schulz-Gasch T, Kusznir E, Muller F, Hennig M, Acta Crystallogr D Biol Crystallogr. 2007 Dec;63(Pt 12):1208-16. Epub 2007, Nov 16. PMID:18084068

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