1EBL

THE 1.8 A CRYSTAL STRUCTURE AND ACTIVE SITE ARCHITECTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE III (FABH) FROM ESCHERICHIA COLI

Summary for 1EBL

• Entry DOI: 10.2210/pdb1ebl/pdb
• Related: 1D9B
• Descriptor: BETA-KETOACYL-ACP SYNTHASE III, COENZYME A (3 entities in total)
• Functional Keywords: acyltransferase, condensing enzyme, fatty acid synthesis, lipid metabolism, alpha-beta protein, five-layered fold, coenzyme a binding protein, helix dipole, malonyl coa decarboxylating enzyme, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm : P0A6R0
• Total number of polymer chains: 2
• Total formula weight: 69381.33

Authors

Davies, C.,Heath, R.J.,White, S.W.,Rock, C.O. (deposition date: 2000-01-24, release date: 2000-02-11, Last modification date: 2024-10-09)

Primary citation

Davies, C.,Heath, R.J.,White, S.W.,Rock, C.O.
The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli.
Structure Fold.Des., 8:185-195, 2000

PubMed Abstract: 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.

PubMed: 10673437
DOI: 10.1016/S0969-2126(00)00094-0

Experimental method

X-RAY DIFFRACTION (1.8 Å)