119th General Meeting of the KCS

Type Poster Presentation
Area 생명화학
Room No. 포스터발표장
Time 4월 21일 (금요일) 13:00~14:30
Code BIO.P-282
Subject NMR Study on Structure of Propionibacterium acnes Acyl Carrier Protein by using NMR Spectroscopy
Authors 천다솜, 이영준1, 김양미*
건국대학교 생명공학과, Korea
1건국대학교 생명특성화대학, Korea
Abstract Acne vulgaris is characterized by inflammatory and non-inflammatory lesions, which are caused by the anaerobic gram-positive bacteria, Propionibacterium acnes. The fatty acid synthesis (FAS) is important for P. acnes and acyl carrier protein (ACP) is an essential part of its FAS. However, the structure of P. acnes ACP has not been studied yet. In this study, P. acnes ACP was cloned and 15N and 13C labeled protein was expressed and purified. We performed 3D NMR experiments and completed backbone assignment. Chemical shift index showed that P. acnes ACP has four α-helices (α1 (I7-T19), α2(S40-F54), α3(D60-N65), and α4(V69-H79)). Using chemical shift perturbation data upon the conversion by covalent modification by a phosphopantetheine prosthetic group, large chemical shift changes near the prosthetic group binding site at Ser40 and the residues (D39, L41, M43, E45, I46, E57, I58) forming a hydrophobic cleft. Using CD spectra, the melting temperature of P. acnes ACP was determined as 61.7°C, which is much lower than those of other ACPs, implying its low thermostability. We performed homology modeling on P. acnes using structure of E.coli ACP as a template and the results agrees well with the chemical shift index data. In our further study, we will determine three-dimensional structure of P. acnes ACP and study it dynamics. Based on these data, we will design inhibitors of FAS protein as a novel antibiotic against P. acnes infection.
E-mail chdasom@konkuk.ac.kr