Chained Structure of Dimeric F₁-like ATPase in Mycoplasma mobile Gliding Machinery.

ABSTRACT: Mycoplasma mobile, a fish pathogen, exhibits gliding motility using ATP hydrolysis on solid surfaces, including animal cells. The gliding machinery can be divided into surface and internal structures. The internal structure of the motor is composed of 28 so-called "chains" that are each composed of 17 repeating protein units called "particles." These proteins include homologs of the catalytic α and β subunits of F₁-ATPase. In this study, we isolated the particles and determined their structures using negative-staining electron microscopy and high-speed atomic force microscopy. The isolated particles were composed of five proteins, MMOB1660 (α-subunit homolog), -1670 (β-subunit homolog), -1630, -1620, and -4530, and showed ATP hydrolyzing activity. The two-dimensional (2D) struct

SUBMITTER: Toyonaga T 

PROVIDER: S-EPMC8406192 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature