The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I |
| |
Authors: | Olsen J G Kadziola A von Wettstein-Knowles P Siggaard-Andersen M Lindquist Y Larsen S |
| |
Affiliation: | 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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |