251946 Acyl Carrier Protein Structural Classification and Normal Mode Analysis

Wednesday, October 31, 2012: 10:36 AM
Washington (Westin )
David C. Cantu, Michael J. Forrester, Katherine Charov and Peter J. Reilly, Chemical and Biological Engineering, Iowa State University, Ames, IA

Acyl carrier proteins (ACP) bind fatty acids and polyketides during their synthesis. They are short proteins composed of antiparallel beta-sheets. All ACPs were gath­ered into the ThYme database, in which enzyme primary and tertiary structures involved in fatty acid and polyketide synthesis and related reactions are tabulated. ACPs are classified into 16 families by amino acid sequence similarity, with members of the different families having sequences with statistically highly significant differences. These classifications are supported by tertiary structure superposition analysis. Tertiary structures from a number of families are very similar, suggesting that these families may come from a single distant ancestor. Normal vibrational mode analysis was conducted on experimentally determined freestanding structures, showing greater fluctuat­ions at chain termini and loops than in most helices. Their modes overlap more so within families than between different families. The tertiary structures of three ACP families that lacked any known structures were predicted as well.

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