FEBS Lett. 1999 Oct 22;460(1):46-52.

The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I.

Olsen JG, Kadziola A, von Wettstein-Knowles P, Siggaard-Andersen M, Lindquist Y, Larsen S.

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Centre for Crystallographic Studies, University of Copenhagen, Denmark.

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.

PMID:: 10571059; [PubMed - indexed for MEDLINE]

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Structures reported by this article

Structure Of E. Coli Kas I H298q Mutant

PDB: 2BZ4

Source: Escherichia coli

Method: X-Ray Diffraction

Resolution: 1.86 Å

See all 6 structures...

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The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I.
The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I.
FEBS Lett. 1999 Oct 22 ;460(1):46-52.

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