+検索条件
-Structure paper
タイトル | Structure of actomyosin rigour complex at 5.2 Å resolution and insights into the ATPase cycle mechanism. |
---|---|
ジャーナル・号・ページ | Nat Commun, Vol. 8, Page 13969, Year 2017 |
掲載日 | 2017年1月9日 |
著者 | Takashi Fujii / Keiichi Namba / |
PubMed 要旨 | Muscle contraction is driven by cyclic association and dissociation of myosin head of the thick filament with thin actin filament coupled with ATP binding and hydrolysis by myosin. However, because ...Muscle contraction is driven by cyclic association and dissociation of myosin head of the thick filament with thin actin filament coupled with ATP binding and hydrolysis by myosin. However, because of the absence of actomyosin rigour structure at high resolution, it still remains unclear how the strong binding of myosin to actin filament triggers the release of hydrolysis products and how ATP binding causes their dissociation. Here we report the structure of mammalian skeletal muscle actomyosin rigour complex at 5.2 Å resolution by electron cryomicroscopy. Comparison with the structures of myosin in various states shows a distinctly large conformational change, providing insights into the ATPase-coupled reaction cycle of actomyosin. Based on our observations, we hypothesize that asymmetric binding along the actin filament could function as a Brownian ratchet by favouring directionally biased thermal motions of myosin and actin. |
リンク | Nat Commun / PubMed:28067235 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 5.2 Å |
構造データ | |
化合物 | ChemComp-ADP: |
由来 |
|
キーワード | MOTOR PROTEIN / Actin / Myosin / Muscle / rigor complex |