The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I |
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Authors: | Olsen J G Kadziola A von Wettstein-Knowles P Siggaard-Andersen M Lindquist Y Larsen S |
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Institution: | Centre for Crystallographic Studies, University of Copenhagen, Denmark. |
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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. |
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