气候变化领域集成服务门户(CCPortal): The myosin II coiled-coil domain atomic structure in its native environment

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DOI	10.1073/pnas.2024151118
	The myosin II coiled-coil domain atomic structure in its native environment
	Rahmani H.; Ma W.; Hu Z.; Daneshparvar N.; Taylor D.W.; McCammon J.A.; Irving T.C.; Edwards R.J.; Taylor K.A.
发表日期	2021
ISSN	00278424
卷号	118 期号:14
英文摘要	The atomic structure of the complete myosin tail within thick filaments isolated from Lethocerus indicus flight muscle is described and compared to crystal structures of recombinant, human cardiac myosin tail segments. Overall, the agreement is good with three exceptions: The proximal S2, in which the filament has heads attached but the crystal structure doesn't, and skip regions 2 and 4. At the head-tail junction, the tail α-helices are asymmetrically structured encompassing well-defined unfolding of 12 residues for one myosin tail, ∼4 residues of the other, and different degrees of α-helix unwinding for both tail α-helices, thereby providing an atomic resolution description of coiled-coil "uncoiling" at the head-tail junction. Asymmetry is observed in the nonhelical C termini; one C-terminal segment is intercalated between ribbons of myosin tails, the other apparently terminating at Skip 4 of another myosin tail. Between skip residues, crystal and filament structures agree well. Skips 1 and 3 also agree well and show the expected α-helix unwinding and coiled-coil untwisting in response to skip residue insertion. Skips 2 and 4 are different. Skip 2 is accommodated in an unusual manner through an increase in α-helix radius and corresponding reduction in rise/residue. Skip 4 remains helical in one chain, with the other chain unfolded, apparently influenced by the acidic myosin C terminus. The atomic model may shed some light on thick filament mechanosensing and is a step in understanding the complex roles that thick filaments of all species undergo during muscle contraction. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Alpha helix coiled coil; Cryo-electron microscopy; Filament; Invertebrate; Striated muscle
语种	英语
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/179970
作者单位	Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306-4380, United States; Department of Physics, Florida State University, Tallahassee, FL 32306-4380, United States; Department of Chemistry and Biochemistry, University of California San Diego, San diego, CA 92093, United States; Department of Biological Sciences, Illinois Institute of Technology, Chicago, IL 60616, United States; Department of Cell Biology, Duke University Medical Center, Durham, NC 27607, United States
推荐引用方式 GB/T 7714	Rahmani H.,Ma W.,Hu Z.,et al. The myosin II coiled-coil domain atomic structure in its native environment[J],2021,118(14).
APA	Rahmani H..,Ma W..,Hu Z..,Daneshparvar N..,Taylor D.W..,...&Taylor K.A..(2021).The myosin II coiled-coil domain atomic structure in its native environment.Proceedings of the National Academy of Sciences of the United States of America,118(14).
MLA	Rahmani H.,et al."The myosin II coiled-coil domain atomic structure in its native environment".Proceedings of the National Academy of Sciences of the United States of America 118.14(2021).