Ion-driven rotary membrane motors: From structure to function

Publikation: Bidrag til tidsskriftReviewForskningfagfællebedømt

Standard

Ion-driven rotary membrane motors : From structure to function. / Martin, Freddie J. O.; Santiveri, Mònica; Hu, Haidai; Taylor, Nicholas M. I.

I: Current Opinion in Structural Biology, Bind 88, 102884, 2024.

Publikation: Bidrag til tidsskriftReviewForskningfagfællebedømt

Harvard

Martin, FJO, Santiveri, M, Hu, H & Taylor, NMI 2024, 'Ion-driven rotary membrane motors: From structure to function', Current Opinion in Structural Biology, bind 88, 102884. https://doi.org/10.1016/j.sbi.2024.102884

APA

Martin, F. J. O., Santiveri, M., Hu, H., & Taylor, N. M. I. (2024). Ion-driven rotary membrane motors: From structure to function. Current Opinion in Structural Biology, 88, [102884]. https://doi.org/10.1016/j.sbi.2024.102884

Vancouver

Martin FJO, Santiveri M, Hu H, Taylor NMI. Ion-driven rotary membrane motors: From structure to function. Current Opinion in Structural Biology. 2024;88. 102884. https://doi.org/10.1016/j.sbi.2024.102884

Author

Martin, Freddie J. O. ; Santiveri, Mònica ; Hu, Haidai ; Taylor, Nicholas M. I. / Ion-driven rotary membrane motors : From structure to function. I: Current Opinion in Structural Biology. 2024 ; Bind 88.

Bibtex

@article{403a0398ea0c40ac830c3b5bf914366b,
title = "Ion-driven rotary membrane motors: From structure to function",
abstract = "Ion-driven membrane motors, essential across all domains of life, convert a gradient of ions across a membrane into rotational energy, facilitating diverse biological processes including ATP synthesis, substrate transport, and bacterial locomotion. Herein, we highlight recent structural advances in the understanding of two classes of ion-driven membrane motors: rotary ATPases and 5:2 motors. The recent structure of the human F-type ATP synthase is emphasised along with the gained structural insight into clinically relevant mutations. Furthermore, we highlight the diverse roles of 5:2 motors and recent mechanistic understanding gained through the resolution of ions in the structure of a sodium-driven motor, combining insights into potential unifying mechanisms of ion selectivity and rotational torque generation in the context of their function as part of complex biological systems.",
author = "Martin, {Freddie J. O.} and M{\`o}nica Santiveri and Haidai Hu and Taylor, {Nicholas M. I.}",
note = "Publisher Copyright: {\textcopyright} 2024 The Author(s)",
year = "2024",
doi = "10.1016/j.sbi.2024.102884",
language = "English",
volume = "88",
journal = "Current Opinion in Structural Biology",
issn = "0959-440X",
publisher = "Elsevier Ltd. * Current Opinion Journals",

}

RIS

TY - JOUR

T1 - Ion-driven rotary membrane motors

T2 - From structure to function

AU - Martin, Freddie J. O.

AU - Santiveri, Mònica

AU - Hu, Haidai

AU - Taylor, Nicholas M. I.

N1 - Publisher Copyright: © 2024 The Author(s)

PY - 2024

Y1 - 2024

N2 - Ion-driven membrane motors, essential across all domains of life, convert a gradient of ions across a membrane into rotational energy, facilitating diverse biological processes including ATP synthesis, substrate transport, and bacterial locomotion. Herein, we highlight recent structural advances in the understanding of two classes of ion-driven membrane motors: rotary ATPases and 5:2 motors. The recent structure of the human F-type ATP synthase is emphasised along with the gained structural insight into clinically relevant mutations. Furthermore, we highlight the diverse roles of 5:2 motors and recent mechanistic understanding gained through the resolution of ions in the structure of a sodium-driven motor, combining insights into potential unifying mechanisms of ion selectivity and rotational torque generation in the context of their function as part of complex biological systems.

AB - Ion-driven membrane motors, essential across all domains of life, convert a gradient of ions across a membrane into rotational energy, facilitating diverse biological processes including ATP synthesis, substrate transport, and bacterial locomotion. Herein, we highlight recent structural advances in the understanding of two classes of ion-driven membrane motors: rotary ATPases and 5:2 motors. The recent structure of the human F-type ATP synthase is emphasised along with the gained structural insight into clinically relevant mutations. Furthermore, we highlight the diverse roles of 5:2 motors and recent mechanistic understanding gained through the resolution of ions in the structure of a sodium-driven motor, combining insights into potential unifying mechanisms of ion selectivity and rotational torque generation in the context of their function as part of complex biological systems.

U2 - 10.1016/j.sbi.2024.102884

DO - 10.1016/j.sbi.2024.102884

M3 - Review

C2 - 39053417

AN - SCOPUS:85199199949

VL - 88

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

SN - 0959-440X

M1 - 102884

ER -

ID: 399963059