Effect of Acylation on the Structure of the Acyl Carrier Protein P

Abstract

Abstract Acyl carrier protein is related with fatty acid biosynthesis in whichspecific enzymes are in-volved. Especially, acyl carrier protein (ACP) is the key component in the growing of fatty acid chain. ACP is the small, very acidic protein that covalently binds various intermediates of fatty acyl chain. Acyl-ation of ACP is mediated by holoacyl carrier protein -synthase (ACPS), which transfers the 4’PP-moiety of CoA to the 36th residue Ser of apoACP. Acyl carrier protein P (ACPP) is one of ACPs from Helicobacter plyori. The NMR structure of ACPP consists of four helices, which were reported previously. Here we show how acylation of ACPP can affect the overall structure of ACPP and figured out the contact surface of ACPP to acyl chain attached during expression of ACPP in E. coli Based on the chemical shift . r- pertubation data, the acylation of ACCP seems to affect the conformation of the long loop connecting helix I and helix II as well as the second short loop connect-ing helix II and helix III. The significant chemical shift change of Ile 54 upon acylation supports the contact of acyl chain and the second loop.