Dataset Information

Structure and dynamics of rotary V1 motor.

ABSTRACT: Rotary ATPases are unique rotary molecular motors that function as energy conversion machines. Among all known rotary ATPases, F1-ATPase is the best characterized rotary molecular motor. There are many high-resolution crystal structures and the rotation dynamics have been investigated in detail by extensive single-molecule studies. In contrast, knowledge on the structure and rotation dynamics of V1-ATPase, another rotary ATPase, has been limited. However, recent high-resolution structural studies and single-molecule studies on V1-ATPase have provided new insights on how the catalytic sites in this molecular motor change its conformation during rotation driven by ATP hydrolysis. In this review, we summarize recent information on the structural features and rotary dynamics of V1-ATPase revealed from structural and single-molecule approaches and discuss the possible chemomechanical coupling scheme of V1-ATPase with a focus on differences between rotary molecular motors.

SUBMITTER: Ueno H

PROVIDER: S-EPMC5910484 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Structure and dynamics of rotary V1 motor.

Ueno Hiroshi H Suzuki Kano K Murata Takeshi T

Cellular and molecular life sciences : CMLS 20180131 10

Rotary ATPases are unique rotary molecular motors that function as energy conversion machines. Among all known rotary ATPases, F1-ATPase is the best characterized rotary molecular motor. There are many high-resolution crystal structures and the rotation dynamics have been investigated in detail by extensive single-molecule studies. In contrast, knowledge on the structure and rotation dynamics of V1-ATPase, another rotary ATPase, has been limited. However, recent high-resolu ...[more]

PMID: 29387903

Similar Datasets

Project description:The membrane-bound component F(0), which is a major component of the F(0)F(1)-ATP synthase, works as a rotary motor and plays a central role in driving the F(1) component to transform chemiosmotic energy into ATP synthesis. We conducted molecular dynamics simulations of b(2)-free F(0) in a 1-palmitoyl-2-oleoyl-phosphatidylcholine lipid bilayer for tens of nanoseconds with two different protonation states of the cAsp-61 residue at the interface of the a-c complex in the absence of electric fields and under electric fields of +/-0.03 V/nm across the membrane. To our surprise, we observed that the upper half of the N-terminal helix of the c(1) subunit rotated about its axis clockwise by 30 degrees . An energetic analysis revealed that the electrostatic repulsion between this N-terminal helix and subunit c(12) was a major contributor to the observed rotation. A correlation map analysis indicated that the correlated motions of residues in the interface of the a-c complex were significantly reduced by external electric fields. The deuterium order parameter (S(CD)) profile calculated by averaging all the lipids in the F(0)-bound bilayer was not very different from that of the pure bilayer system, in agreement with recent (2)H solid-state NMR experiments. However, by delineating the lipid properties according to their vicinity to F(0), we found that the S(CD) profiles of different lipid shells were prominently different. Lipids close to F(0) formed a more ordered structure. Similarly, the lateral diffusion of lipids on the membrane surface also followed a shell-dependent behavior. The lipids in the proximity of F(0) exhibited very significantly reduced diffusional motion. The numerical value of S(CD) was anticorrelated with that of the diffusion coefficient, i.e., the more ordered lipid structures led to slower lipid diffusion. Our findings will help elucidate the dynamics of F(0) depending on the protonation state and electric field, and may also shed some light on the interactions between the motor F(0) and its surrounding lipids under physiological conditions, which could help to rationalize its extraordinary energy conversion efficiency.

Dataset Information

Structure and dynamics of rotary V1 motor.

Publications

Structure and dynamics of rotary V<sub>1</sub> motor.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets