Structure of F-ATPase from the Obligate Anaerobe Fusobacterium Nucleatum

Overview

Journal Open Biol

Specialties Biology
Cell Biology
Molecular Biology

Date 2019 Jun 27

PMID 31238823

Citations 1

Authors

Jessica Petri

Yoshio Nakatani

Martin G Montgomery

Scott A Ferguson

David Aragao

Andrew G W Leslie

Adam Heikal

John E Walker

Gregory M Cook

Affiliations

Soon will be listed here.

Abstract

The crystal structure of the F-catalytic domain of the adenosine triphosphate (ATP) synthase has been determined from the pathogenic anaerobic bacterium Fusobacterium nucleatum. The enzyme can hydrolyse ATP but is partially inhibited. The structure is similar to those of the F-ATPases from Caldalkalibacillus thermarum, which is more strongly inhibited in ATP hydrolysis, and in Mycobacterium smegmatis, which has a very low ATP hydrolytic activity. The β-subunits in all three enzymes are in the conventional 'open' state, and in the case of C. thermarum and M. smegmatis, they are occupied by an ADP and phosphate (or sulfate), but in F. nucleatum, the occupancy by ADP appears to be partial. It is likely that the hydrolytic activity of the F. nucleatum enzyme is regulated by the concentration of ADP, as in mitochondria.

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