中国物理B ›› 2005, Vol. 14 ›› Issue (11): 2214-2221.doi: 10.1088/1009-1963/14/11/012

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Numerical study of the coupling between F0 with varied numbers of c-subunits and F1 in an ATP synthase

钱钧, 谢平, 窦硕星, 王鹏业   

  1. Laboratory of Soft Matter Physics, Beijing National Laboratory for Condensed Matter Physics,Institute of Physics, Chinese Academy of Sciences, Beijing 100080, China
  • 收稿日期:2005-03-18 修回日期:2005-08-19 出版日期:2005-11-20 发布日期:2005-11-20
  • 基金资助:
    Project supported by the National Natural Science Foundation of China (Grant Nos 60025516 and 10334100).

Numerical study of the coupling between F0 with varied numbers of c-subunits and F1 in an ATP synthase

Qian Jun (钱钧), Xie Ping (谢平), Dou Shuo-Xing (窦硕星), Wang Peng-Ye (王鹏业)   

  1. Laboratory of Soft Matter Physics, Beijing National Laboratory for Condensed Matter Physics,Institute of Physics, Chinese Academy of Sciences, Beijing 100080, China
  • Received:2005-03-18 Revised:2005-08-19 Online:2005-11-20 Published:2005-11-20
  • Supported by:
    Project supported by the National Natural Science Foundation of China (Grant Nos 60025516 and 10334100).

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摘要： ATP synthase is a rotary motor which is composed of two portions: the `rotor' F0, consisting of a c-ring, and the `stator' F1, consisting of an \alpha3\beta3 hexamer. In different species, the number of c-subunits which form the c-ring is varied from 10 to 14, whereas the \alpha3 \beta3 hexamer is fixed to be 3-fold symmetrical. We have numerically studied the rotational coupling between F0 with varied number of c-subunits and F1. It is found that, for any number of c-subunits, the rotor F0 advances 3 steps per revolution on average, which is determined by the period of F1, whereas the exact angular pausing positions are determined by the period of F0. When the symmetry of the c-ring of F0 is matched with the 3-fold symmetry of F1, the three steps have equivalent sizes. If not matched, the three steps become nonequivalent: both the step size and average dwell time are different for these steps.

关键词: ATP synthase, rotational coupling, numerical simulation

Abstract: ATP synthase is a rotary motor which is composed of two portions: the `rotor' F0, consisting of a c-ring, and the `stator' F1, consisting of an $\alpha$3$\beta$3 hexamer. In different species, the number of c-subunits which form the c-ring is varied from 10 to 14, whereas the $\alpha$3$\beta$3 hexamer is fixed to be 3-fold symmetrical. We have numerically studied the rotational coupling between F0 with varied number of c-subunits and F1. It is found that, for any number of c-subunits, the rotor F0 advances 3 steps per revolution on average, which is determined by the period of F1, whereas the exact angular pausing positions are determined by the period of F0. When the symmetry of the c-ring of F0 is matched with the 3-fold symmetry of F1, the three steps have equivalent sizes. If not matched, the three steps become nonequivalent: both the step size and average dwell time are different for these steps.

Key words: ATP synthase, rotational coupling, numerical simulation

中图分类号:  (Structure of biomolecules)

  • 87.15.B-
87.15.H- (Dynamics of biomolecules) 87.15.K- (Molecular interactions; membrane-protein interactions) 87.15.Cc (Folding: thermodynamics, statistical mechanics, models, and pathways) 87.14.E- (Proteins)