1FMW

CRYSTAL STRUCTURE OF THE MGATP COMPLEX FOR THE MOTOR DOMAIN OF DICTYOSTELIUM MYOSIN II

1FMW の概要

• エントリーDOI: 10.2210/pdb1fmw/pdb
• 関連するPDBエントリー: 1FMW 1MMD 1MND
• 分子名称: MYOSIN II HEAVY CHAIN, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: myosin motor domaim, contractile protein
• 由来する生物種: Dictyostelium discoideum
• 細胞内の位置: Cytoplasm, cell cortex: P08799
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 87252.57

構造登録者

Bauer, C.B.,Holden, H.M.,Thoden, J.B.,Smith, R.,Rayment, I. (登録日: 2000-08-18, 公開日: 2000-11-22, 最終更新日: 2024-02-07)

主引用文献

Bauer, C.B.,Holden, H.M.,Thoden, J.B.,Smith, R.,Rayment, I.
X-ray structures of the apo and MgATP-bound states of Dictyostelium discoideum myosin motor domain.
J.Biol.Chem., 275:38494-38499, 2000

PubMed Abstract: Myosin is the most comprehensively studied molecular motor that converts energy from the hydrolysis of MgATP into directed movement. Its motile cycle consists of a sequential series of interactions between myosin, actin, MgATP, and the products of hydrolysis, where the affinity of myosin for actin is modulated by the nature of the nucleotide bound in the active site. The first step in the contractile cycle occurs when ATP binds to actomyosin and releases myosin from the complex. We report here the structure of the motor domain of Dictyostelium discoideum myosin II both in its nucleotide-free state and complexed with MgATP. The structure with MgATP was obtained by soaking the crystals in substrate. These structures reveal that both the apo form and the MgATP complex are very similar to those previously seen with MgATPgammaS and MgAMP-PNP. Moreover, these structures are similar to that of chicken skeletal myosin subfragment-1. The crystallized protein is enzymatically active in solution, indicating that the conformation of myosin observed in chicken skeletal myosin subfragment-1 is unable to hydrolyze ATP and most likely represents the pre-hydrolysis structure for the myosin head that occurs after release from actin.

PubMed: 10954715
DOI: 10.1074/jbc.M005585200

実験手法

X-RAY DIFFRACTION (2.15 Å)