JKMRS Volume 19, No 3, pp 149; Effect of Acylation on the Stru... | |
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2015년 12월 19일 / 조회수: 621 | |
Effect of Acylation on the Structure of
the Acyl Carrier Protein P Ja-shil Hyun* and Sung Jean Park* College of Pharmacy, Gachon University, 534-2
Yeonsu-dong, Yeonsu-gu, Incheon, Republic of Korea Received Oct 03, 2015; Revised Nov 15, 2015; Accepted Nov 25, 2015
Abstract Acyl carrier protein is related with fatty acid biosynthesis
in which specific enzymes are involved. 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.
Acylation of ACP is mediated by holo-acyl carrier protein synthase (ACPS),
which transfers the 4’PP-moiety of CoA to the 36th residue Ser of apo ACP. 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 perturbation 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 connecting 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.
Keywords Acyl carrier protein, ACPP, Acylation, fatty acid biosynthesis, Structure, NMR |
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