Chained Structure of Dimeric F <sub>1</sub> -like ATPase in Mycoplasma mobile Gliding Machinery
Takuma Toyonaga, Takayuki Kato, Akihiro Kawamoto, Noriyuki Kodera, Tasuku Hamaguchi, Yuhei O. Tahara, Toshio Ando, Keiichi Namba, Makoto Miyata
Abstract
F 1 F o -ATPase, a rotary ATPase, is widespread in the membranes of mitochondria, chloroplasts, and bacteria and converts ATP energy with a proton motive force across the membrane by its physical rotation. Homologous protein complexes play roles in ion and protein transport. Mycoplasma mobile , a pathogenic bacterium, was recently suggested to have a special motility system evolutionarily derived from F 1 -ATPase.
Topics & Concepts
Negative stainATPaseDimerAAA proteinsProtein subunitChemistryBiophysicsCrystallographyMotor proteinATP hydrolysisActinBiochemistryBiologyCell biologyEnzymeElectron microscopeMicrotubuleGenePhysicsOpticsOrganic chemistryATP Synthase and ATPases ResearchForce Microscopy Techniques and ApplicationsLipid Membrane Structure and Behavior