The X‐ray crystal structure of β‐ketoacyl [acyl carrier protein] synthase I
- 22 October 1999
- journal article
- Published by Wiley in FEBS Letters
- Vol. 460 (1) , 46-52
- https://doi.org/10.1016/s0014-5793(99)01303-4
Abstract
The crystal structure of the fatty acid elongating enzyme β‐ketoacyl [acyl carrier protein] synthase I (KAS I) from Escherichia coli has been determined to 2.3 Å 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 αβαβα 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
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