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제109회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Differences in Conformations and Dynamics of Apo, Holo and Acyl Forms of Acyl Carrier Protein

2012년 2월 22일 19시 52분 20초
PHYS.P-506 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
4월 25일 (수요일) 18:00~21:00
저자 및
정기웅, 김진경, 강동일1, 김양미
건국대학교 생명공학과, Korea
1건국대학교 화학과, Korea
Acyl carrier protein (ACP) is a small (~9 kDa) acidic protein whose function is essential for numerous biosynthetic pathways that depend upon acyl group transfer. We investigated structure and dynamic properties of apo, holo, acyl-ACP from Escherichia coli. From the observation of chemical shift variations, we confirmed that apo-ACP show only one conformation, while, holo-ACP with Ca2+ showed two sets of resonances, suggesting that two conformers are in dynamic equilibrium. Also, NMR data of acyl-ACP revealed that changes in the length of the covalently attached fatty acid affect the local conformation and the dynamics of ACP. Acylation stabilizes one conformation and model-free analysis comparing butyryl-, hexanoyl-and octanoyl-ACP indicated that ACP showed increase of structural rigidity upon binding to longer acyl chain. Studies on the interactions between acyl-ACP and the enzymes in FAS such as β-ketoacyl-acyl carrier protein synthase III and β-ketoacyl-acyl carrier protein reductase, showed that large chemical shift perturbations were observed for negatively charged residues in second helix of acyl-ACP, suggesting that the electrostatic interactions between acyl-ACP and enzymes in FAS are important for elongation reactions of acyl chains.