Solution Structure of Acyl Carrier Protein

Abstract

The role of acyl carrier protein (ACP) in the biosynthesis of membrane lipid precursors is well established (for review see Vagelos, 1971, 1973; Prescott and Vagelos, 1972). ACP and its thioesters interact specifically with at least a dozen enzymes of fatty acid biosynthesis in Escherichia coli, and acyl-ACPs are substrates for the sn-glycerol-3-phosphate acyltransferase. The complete primary structure of ACP is known (Vanaman et al., 1968). The molecular weight is 8847, and the protein contains a 4′-phosphopantetheine moiety as a prosthetic group attached via a phosphodiester linkage to Ser 36. The acyl intermediates are attached as thioesters to the terminal sulfhydryl of the prosthetic group. Recent work on the regulation of membrane lipid biogenesis has focused attention on several enzyme systems that utilize acyl-ACP substrates. The involvement of ACP in these pathways has renewed interest in the solution structure of ACP and how it relates to the biochemical behavior of this protein. The purpose of this chapter is to summarize and review recent experimental findings on the structure of ACP particularly with regard to lipid-protein interactions.