1F91

BETA-KETOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE I IN COMPLEX WITH C10 FATTY ACID SUBSTRATE

Summary for 1F91

• Entry DOI: 10.2210/pdb1f91/pdb
• Related: 1DD8 1EK4
• Descriptor: BETA-KETOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE I, HYDROXIDE ION, DECANOIC ACID, ... (4 entities in total)
• Functional Keywords: thiolase fold family, dimer, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A953
• Total number of polymer chains: 4
• Total formula weight: 171429.85

Authors

Olsen, J.G.,Kadziola, A.,Wettstein-Knowles, P.V.,Siggaard-Andersen, M.,Larsen, S. (deposition date: 2000-07-06, release date: 2001-04-11, Last modification date: 2024-11-20)

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 (2.4 Å)