Origin of the Surprising Mechanical Stability of Kinesin's Neck Coiled Coil

doi:10.1021/acs.jctc.0c00566

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	Origin of the Surprising Mechanical Stability of Kinesin's Neck Coiled Coil
	Liu, Shu-Xia ; Lu, Gang 4; Zhang, Hui ; Geng, Yi-Zhao ; Jix, Qing 2,3
刊名	JOURNAL OF CHEMICAL THEORY AND COMPUTATION
	2021
卷号	17 期号:2 页码:1017-1029
ISSN号	1549-9618
DOI	10.1021/acs.jctc.0c00566
英文摘要	Kinesin-1 is a motor protein moving along a microtubule with its two identical motor heads dimerized by two neck linkers and a coiled-coil stalk. When both motor heads bind the microtubule, an internal strain is built up between the two heads, which is indispensable to ensure proper coordination of the two motor heads during kinesin-1's mechanochemical cycle. The internal strain forms a tensile force along the neck linker that tends to unwind the neck coiled coil (NCC). Experiments showed that the kinesin-1's NCC has a high antiunwinding ability compared with conventional coiled coils, which was mainly attributed to the enhanced hydrophobic pressure arising from the unconventional sequence of kinesin-1's NCC. However, hydrophobic pressure cannot provide the shearing force which is needed to balance the tensile force on the interface between two helices. To find out the true origin of the mechanical stability of kinesin-1's NCC, we perform a novel and detailed mechanical analysis for the system based on molecular dynamics simulation at an atomic level. We find that the needed shearing force is provided by a buckle structure formed by two tyrosines which form effective steric hindrance in the presence of tensile forces. The tensile force is balanced by the tensile direction component of the contact force between the two tyrosines which forms the shearing force. The hydrophobic pressure balances the other component of the contact force perpendicular to the tensile direction. The antiunwinding strength of NCC is defined by the maximum shearing force, which is finally determined by the hydrophobic pressure. Kinesin-1 uses residues with plane side chains, tryptophans and tyrosines, to form the hydrophobic center and to shorten the interhelix distance so that a high antiunwinding strength is obtained. The special design of NCC ensures exquisite cooperation of steric hindrance and hydrophobic pressure that results in the surprising mechanical stability of NCC.
学科主题	Chemistry ; Physics
语种	英语
内容类型	期刊论文
源URL	[http://ir.itp.ac.cn/handle/311006/27643]
专题	理论物理研究所_理论物理所1978-2010年知识产出
作者单位	1.Chinese Acad Sci, Inst Theoret Phys, State Key Lab Theoret Phys, Beijing 100190, Peoples R China 2.North China Elect Power Univ, Math & Phys Sci Sch, Baoding 071003, Peoples R China 3.Hebei Univ Technol, Sch Sci, Tianjin 300401, Peoples R China 4.Hebei Univ Technol, Inst Biophys, Tianjin 300401, Peoples R China
推荐引用方式 GB/T 7714	Liu, Shu-Xia,Lu, Gang,Zhang, Hui,et al. Origin of the Surprising Mechanical Stability of Kinesin's Neck Coiled Coil[J]. JOURNAL OF CHEMICAL THEORY AND COMPUTATION,2021,17(2):1017-1029.
APA	Liu, Shu-Xia,Lu, Gang,Zhang, Hui,Geng, Yi-Zhao,&Jix, Qing.(2021).Origin of the Surprising Mechanical Stability of Kinesin's Neck Coiled Coil.JOURNAL OF CHEMICAL THEORY AND COMPUTATION,17(2),1017-1029.
MLA	Liu, Shu-Xia,et al."Origin of the Surprising Mechanical Stability of Kinesin's Neck Coiled Coil".JOURNAL OF CHEMICAL THEORY AND COMPUTATION 17.2(2021):1017-1029.