Structural modification of acyl carrier protein by butyryl group.
Fatty acid synthesis in bacteria is catalyzed by a set of individual enzymes known as the type II fatty acid synthase. Acyl carrier protein (ACP) shuttles the acyl intermediates between individual pathway enzymes. In this study, we determined the solution structures of three different forms of ACP, apo-ACP, ACP, and butyryl-ACP under identical experimental conditions. The structural studies revealed that attachment of butyryl acyl intermediate to ACP alters the conformation of ACP. This finding supports the more general notion that the attachment of different acyl intermediates alters the ACP structure to facilitate their recognition and turnover by the appropriate target enzymes.
Wu
Bai-Nan
BN
Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, USA.
Zhang
Yong-Mei
YM
Rock
Charles O
CO
Zheng
Jie J
JJ
D000213:Acyl Carrier Protein / Q000737:chemistry* / Q000378:metabolism*; D001059:Apoproteins / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D054889:Fatty Acid Synthase, Type II; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010204:Pantetheine / Q000031:analogs & derivatives / Q000378:metabolism; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity
D000213:Acyl Carrier Protein; D001059:Apoproteins; D029968:Escherichia coli Proteins; C040157:acpP protein, E coli; D010204:Pantetheine; D054889:Fatty Acid Synthase, Type II; C003129:4'-phosphopantetheine