Bacterial F-type ATP synthases follow a well-choreographed assembly pathway

Khanh Vu Huu; Rene Zangl; Jan Hoffmann; Alicia Just; Nina Morgner

doi:10.1038/s41467-022-28828-1

Nature Communications (Mar 2022)

Bacterial F-type ATP synthases follow a well-choreographed assembly pathway

Khanh Vu Huu,
Rene Zangl,
Jan Hoffmann,
Alicia Just,
Nina Morgner

Affiliations

Khanh Vu Huu: Institute of Physical and Theoretical Chemistry, Goethe University Frankfurt/Main
Rene Zangl: Institute of Physical and Theoretical Chemistry, Goethe University Frankfurt/Main
Jan Hoffmann: Institute of Physical and Theoretical Chemistry, Goethe University Frankfurt/Main
Alicia Just: Institute of Physical and Theoretical Chemistry, Goethe University Frankfurt/Main
Nina Morgner: Institute of Physical and Theoretical Chemistry, Goethe University Frankfurt/Main

DOI: https://doi.org/10.1038/s41467-022-28828-1
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 13

Abstract

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ATPases are the macromolecular machines for cellular energy production. Here the authors investigate factors that govern the assembly of the F1 complex from a bacterial F-type ATPase and relate differences in activity of complexes assembled in cells and in vitro to structural changes.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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