1ebl
From Proteopedia
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|PDB= 1ebl |SIZE=350|CAPTION= <scene name='initialview01'>1ebl</scene>, resolution 1.8Å | |PDB= 1ebl |SIZE=350|CAPTION= <scene name='initialview01'>1ebl</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=COA:COENZYME A'>COA</scene> | + | |LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
| - | |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=[[1d9b|1D9B]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ebl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ebl OCA], [http://www.ebi.ac.uk/pdbsum/1ebl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ebl RCSB]</span> | ||
}} | }} | ||
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[[Category: Rock, C O.]] | [[Category: Rock, C O.]] | ||
[[Category: White, S W.]] | [[Category: White, S W.]] | ||
| - | [[Category: COA]] | ||
[[Category: acyltransferase]] | [[Category: acyltransferase]] | ||
[[Category: alpha-beta protein]] | [[Category: alpha-beta protein]] | ||
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[[Category: malonyl coa decarboxylating enzyme]] | [[Category: malonyl coa decarboxylating enzyme]] | ||
| - | ''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 19:59:18 2008'' |
Revision as of 16:59, 30 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 | ||||||
| Related: | 1D9B
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE 1.8 A CRYSTAL STRUCTURE AND ACTIVE SITE ARCHITECTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE III (FABH) FROM ESCHERICHIA COLI
Overview
Background: beta-Ketoacyl-acyl carrier protein synthase III (FabH) initiates elongation in type II fatty acid synthase systems found in bacteria and plants. FabH is a ubiquitous component of the type II system and is positioned ideally in the pathway to control the production of fatty acids. The elucidation of the structure of FabH is important for the understanding of its regulation by feedback inhibition and its interaction with drugs. Although the structures of two related condensing enzymes are known, the roles of the active-site residues have not been experimentally tested. Results: The 1.8 A crystal structure of FabH was determined using a 12-site selenium multiwavelength anomalous dispersion experiment. The active site (Cys112, His244 and Asn274) is formed by the convergence of two alpha helices and is accessed via a narrow hydrophobic tunnel. Hydrogen-bonding networks that include two tightly bound water molecules fix the positions of His244 and Asn274, which are critical for the decarboxylation and condensation reactions. Surprisingly, the His244-->Ala mutation does not affect the transacylation reaction suggesting that His244 has only a minor influence on the nucleophilicity of Cys112. Conclusions: The histidine and asparagine active-site residues are both required for the decarboxylation step in the condensation reaction. The nucleophilicity of the active-site cysteine is enhanced by the alpha-helix dipole effect, and an oxyanion hole promotes the formation of the tetrahedral transition state.
About this Structure
1EBL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli., Davies C, Heath RJ, White SW, Rock CO, Structure. 2000 Feb 15;8(2):185-95. PMID:10673437
Page seeded by OCA on Sun Mar 30 19:59:18 2008
Categories: Beta-ketoacyl-acyl-carrier-protein synthase I | Escherichia coli | Single protein | Davies, C. | Heath, R J. | Rock, C O. | White, S W. | Acyltransferase | Alpha-beta protein | Coenzyme a binding protein | Condensing enzyme | Fatty acid synthesis | Five-layered fold | Helix dipole | Lipid metabolism | Malonyl coa decarboxylating enzyme
