1EK4

BETA-KETOACYL [ACYL CARRIER PROTEIN] SYNTHASE I IN COMPLEX WITH DODECANOIC ACID TO 1.85 RESOLUTION

Summary for 1EK4

• Entry DOI: 10.2210/pdb1ek4/pdb
• Related: 1dd8
• Descriptor: BETA-KETOACYL [ACYL CARRIER PROTEIN] SYNTHASE I, LAURIC ACID (3 entities in total)
• Functional Keywords: fatty acid synthase, thiolase fold, claisen condensation, fatty acid substrate complex, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A953
• Total number of polymer chains: 4
• Total formula weight: 177096.10

Authors

Olsen, J.G.,Kadziola, A.,Siggaard-Andersen, M.,von Wettstein-Knowles, P.,Larsen, S. (deposition date: 2000-03-06, release date: 2001-04-11, Last modification date: 2024-10-30)

Primary citation

Olsen, J.G.,Kadziola, A.,von Wettstein-Knowles, P.,Siggaard-Andersen, M.,Larsen, S.
Structures of beta-ketoacyl-acyl carrier protein synthase I complexed with fatty acids elucidate its catalytic machinery.
Structure, 9:233-243, 2001

PubMed Abstract: beta-ketoacyl-acyl carrier protein synthase (KAS) I is vital for the construction of the unsaturated fatty acid carbon skeletons characterizing E. coli membrane lipids. The new carbon-carbon bonds are created by KAS I in a Claisen condensation performed in a three-step enzymatic reaction. KAS I belongs to the thiolase fold enzymes, of which structures are known for five other enzymes.

PubMed: 11286890
DOI: 10.1016/S0969-2126(01)00583-4

Experimental method

X-RAY DIFFRACTION (1.85 Å)