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-Structure paper
タイトル | Structural basis for cofilin binding and actin filament disassembly. |
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ジャーナル・号・ページ | Nat Commun, Vol. 9, Issue 1, Page 1860, Year 2018 |
掲載日 | 2018年5月10日 |
著者 | Kotaro Tanaka / Shuichi Takeda / Kaoru Mitsuoka / Toshiro Oda / Chieko Kimura-Sakiyama / Yuichiro Maéda / Akihiro Narita / |
PubMed 要旨 | Actin depolymerizing factor (ADF) and cofilin accelerate actin dynamics by severing and disassembling actin filaments. Here, we present the 3.8 Å resolution cryo-EM structure of cofilactin ...Actin depolymerizing factor (ADF) and cofilin accelerate actin dynamics by severing and disassembling actin filaments. Here, we present the 3.8 Å resolution cryo-EM structure of cofilactin (cofilin-decorated actin filament). The actin subunit structure of cofilactin (C-form) is distinct from those of F-actin (F-form) and monomeric actin (G-form). During the transition between these three conformations, the inner domain of actin (subdomains 3 and 4) and the majority of subdomain 1 move as two separate rigid bodies. The cofilin-actin interface consists of three distinct parts. Based on the rigid body movements of actin and the three cofilin-actin interfaces, we propose models for the cooperative binding of cofilin to actin, preferential binding of cofilin to ADP-bound actin filaments and cofilin-mediated severing of actin filaments. |
リンク | Nat Commun / PubMed:29749375 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 3.8 Å |
構造データ | |
化合物 | ChemComp-MG: ChemComp-ADP: |
由来 |
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キーワード | CYTOSOLIC PROTEIN / Actin / Cofilin / muscle / cytoskeleton |