1LKX
MOTOR DOMAIN OF MYOE, A CLASS-I MYOSIN
1LKX の概要
| エントリーDOI | 10.2210/pdb1lkx/pdb |
| 分子名称 | MYOSIN IE HEAVY CHAIN, MAGNESIUM ION, VANADATE ION, ... (5 entities in total) |
| 機能のキーワード | myosin motor domain, lever arm, converter domain, contractile protein |
| 由来する生物種 | Dictyostelium discoideum |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 318926.87 |
| 構造登録者 | Kollmar, M.,Durrwang, U.,Kliche, W.,Manstein, D.J.,Kull, F.J. (登録日: 2002-04-26, 公開日: 2002-06-26, 最終更新日: 2024-02-14) |
| 主引用文献 | Kollmar, M.,Durrwang, U.,Kliche, W.,Manstein, D.J.,Kull, F.J. Crystal structure of the motor domain of a class-I myosin. EMBO J., 21:2517-2525, 2002 Cited by PubMed Abstract: The crystal structure of the motor domain of Dictyostelium discoideum myosin-IE, a monomeric unconventional myosin, was determined. The crystallographic asymmetric unit contains four independently resolved molecules, highlighting regions that undergo large conformational changes. Differences are particularly pronounced in the actin binding region and the converter domain. The changes in position of the converter domain reflect movements both parallel to and perpendicular to the actin axis. The orientation of the converter domain is approximately 30 degrees further up than in other myosin structures, indicating that MyoE can produce a larger power stroke by rotating its lever arm through a larger angle. The role of extended loops near the actin-binding site is discussed in the context of cellular localization. The core regions of the motor domain are similar, and the structure reveals how that core is stabilized in the absence of an N-terminal SH3-like domain. PubMed: 12032065DOI: 10.1093/emboj/21.11.2517 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3 Å) |
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