Intein-mediated cyclization of bacterial acyl carrier protein stabilizes its folded conformation but does not abolish function.

ABSTRACT: Bacterial acyl carrier protein (ACP) is essential for the synthesis of fatty acids and serves as the major acyl donor for the formation of phospholipids and other lipid products. Acyl-ACP encloses attached fatty acyl groups in a hydrophobic pocket within a four-helix bundle, but must at least partially unfold to present the acyl chain to the active sites of its multiple enzyme partners. To further examine the constraints of ACP structure and function, we have constructed a cyclic version of Vibrio harveyi ACP, using split-intein technology to covalently join its closely apposed N and C termini. Cyclization stabilized ACP in a folded helical conformation as indicated by gel electrophoresis, circular dichroism, fluorescence, and mass spectrometry. Molecular dynamics simulations also indicate

SUBMITTER: Volkmann G 

PROVIDER: S-EPMC2838282 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature