Structural analysis of myosin II subfragment 1 decorated actin filament by CryoEM
| Project/Area Number |
23770179
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biophysics
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| Research Institution | The Institute of Physical and Chemical Research (2012)
Osaka University (2011) |
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Principal Investigator |
FUJII Takashi 独立行政法人理化学研究所, 細胞動態計測研究グループ, 基礎科学特別研究員 (10582611)
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| Project Period (FY) |
2011 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2012: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2011: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | 低温電子顕微鏡法 / アクチン / ミオシン / 筋肉 |
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| Research Abstract |
To understand the mechanism of muscle contraction,it is necessary to reveal how myosin binds to actin. Despite tons of biochemical information, the detail structure of actin-myosin complex remains unknown. We have obtained 7Å resolution density map of actin-myosin II S1 rigor complex by CryoEM. The density map clearly resolves all the secondary structures, such as α-helices, β-structures and loops, having made unambiguous modeling and refinement possible. The structure suggests that myosin undergoes a drastic conformational change upon strongly binding to the actin filament and that a myosin binds to two actin monomers. The high resolution structure gave us a relative three dimensional arrangement between actin and myosin, suggesting that the mutations caused myopathic illness is highly related to the residues forming the actin-myosin interface.
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Report
(3 results)
Research Products
(8 results)
