2BKH
Myosin VI nucleotide-free (MDInsert2) crystal structure
2BKH の概要
| エントリーDOI | 10.2210/pdb2bkh/pdb |
| 関連するPDBエントリー | 1MXE 2BBM 2BBN 2BKI 4CLN |
| 分子名称 | UNCONVENTIONAL MYOSIN, CALMODULIN, GLYCEROL, ... (5 entities in total) |
| 機能のキーワード | motor protein/metal-binding protein, complex (motor protein-calmodulin), myosin vi, reverse myosin, calmodulin, non-conventional myosin, nucleotide-free conformation, muscle protein, motor protein-metal-binding protein complex |
| 由来する生物種 | SUS SCROFA (PIG) 詳細 |
| 細胞内の位置 | Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein (By similarity): Q29122 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 110571.47 |
| 構造登録者 | Menetrey, J.,Bahloul, A.,Yengo, C.,Wells, A.,Morris, C.,Sweeney, H.L.,Houdusse, A. (登録日: 2005-02-16, 公開日: 2005-06-07, 最終更新日: 2023-12-13) |
| 主引用文献 | Menetrey, J.,Bahloul, A.,Wells, A.,Yengo, C.,Morris, C.,Sweeney, H.L.,Houdusse, A. The Structure of the Myosin Vi Motor Reveals the Mechanism of Directionality Reversal Nature, 435:779-, 2005 Cited by PubMed Abstract: Here we solve a 2.4-A structure of a truncated version of the reverse-direction myosin motor, myosin VI, that contains the motor domain and binding sites for two calmodulin molecules. The structure reveals only minor differences in the motor domain from that in plus-end directed myosins, with the exception of two unique inserts. The first is near the nucleotide-binding pocket and alters the rates of nucleotide association and dissociation. The second unique insert forms an integral part of the myosin VI converter domain along with a calmodulin bound to a novel target motif within the insert. This serves to redirect the effective 'lever arm' of myosin VI, which includes a second calmodulin bound to an 'IQ motif', towards the pointed (minus) end of the actin filament. This repositioning largely accounts for the reverse directionality of this class of myosin motors. We propose a model incorporating a kinesin-like uncoupling/docking mechanism to provide a full explanation of the movements of myosin VI. PubMed: 15944696DOI: 10.1038/NATURE03592 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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