1DD8

CRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I FROM ESCHERICHIA COLI

Summary for 1DD8

• Entry DOI: 10.2210/pdb1dd8/pdb
• Descriptor: BETA-KETOACYL [ACYL CARRIER PROTEIN] SYNTHASE I (2 entities in total)
• Functional Keywords: thiolase fold, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A953
• Total number of polymer chains: 4
• Total formula weight: 170737.02

Authors

Olsen, J.G.,Kadziola, A.,von Wettstein-Knowles, P.,Siggaard-Andersen, M.,Lindquist, Y.,Larsen, S. (deposition date: 1999-11-09, release date: 1999-11-18, Last modification date: 2024-02-07)

Primary citation

Olsen, J.G.,Kadziola, A.,von Wettstein-Knowles, P.,Siggaard-Andersen, M.,Lindquist, Y.,Larsen, S.
The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I.
FEBS Lett., 460:46-52, 1999

PubMed Abstract: The crystal structure of the fatty acid elongating enzyme beta-ketoacyl [acyl carrier protein] synthase I (KAS I) from Escherichia coli has been determined to 2.3 A resolution by molecular replacement using the recently solved crystal structure of KAS II as a search model. The crystal contains two independent dimers in the asymmetric unit. KAS I assumes the thiolase alpha(beta)alpha(beta)alpha fold. Electrostatic potential distribution reveals an acyl carrier protein docking site and a presumed substrate binding pocket was detected extending the active site. Both subunits contribute to each substrate binding site in the dimer.

PubMed: 10571059
DOI: 10.1016/S0014-5793(99)01303-4

Experimental method

X-RAY DIFFRACTION (2.3 Å)