The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I.
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Olsen JG, 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. 1999 Oct 22;460(1):46-52.
- PubMed ID
- 10571059 [ View in 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.