F1-ATP酶构象变化旋转机制的动力学分析。

A dynamic analysis of the rotation mechanism for conformational change in F(1)-ATPase.

作者信息

Ma Jianpeng, Flynn Terence C, Cui Qiang, Leslie Andrew G W, Walker John E, Karplus Martin

机构信息

Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, BCM-125, Houston, TX 77030, USA.

出版信息

Structure. 2002 Jul;10(7):921-31. doi: 10.1016/s0969-2126(02)00789-x.

DOI:10.1016/s0969-2126(02)00789-x

PMID:12121647

Abstract

Molecular dynamics trajectories for the bovine mitochondrial F(1)-ATPase are used to demonstrate the motions and interactions that take place during the elementary (120 degrees rotation) step of the gamma subunit. The results show how rotation of the gamma subunit induces the observed structural changes in the catalytic beta subunits. Both steric and electrostatic interactions contribute. An "ionic track" of Arg and Lys residues on the protruding portion of the gamma subunit plays a role in guiding the motions of the beta subunits. Experimental data for mutants of the DELSEED motif and the hinge region are interpreted on the basis of the molecular dynamics results. The trajectory provides a unified dynamic description of the coupled subunit motions involved in the 120 degrees rotation cycles of F(1)-ATPase.

摘要

牛线粒体F(1)-ATP合酶的分子动力学轨迹用于展示γ亚基基本（120度旋转）步骤中发生的运动和相互作用。结果表明γ亚基的旋转如何诱导催化β亚基中观察到的结构变化。空间和静电相互作用都有贡献。γ亚基突出部分上的精氨酸和赖氨酸残基的“离子轨迹”在引导β亚基的运动中起作用。基于分子动力学结果解释了DELSEED基序和铰链区突变体的实验数据。该轨迹为F(1)-ATP合酶120度旋转循环中涉及的亚基耦合运动提供了统一的动态描述。