期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 17, 期 3, 页码 373-U145出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1761
关键词
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资金
- US Department of Energy, Basic Energy Sciences, Office of Science [DE-AC02-06CH11357]
- National Institutes of Health, National Center for Research Resources [RR007707]
- National Cancer Institute [Y1-CO-1020]
- National Institute of General Medical Science [Y1-GM-1104]
- Australian Nuclear Science Technology Organization
- Australian National Health & Medical Research Council [DP573712]
- MRC [MC_U105170645] Funding Source: UKRI
- Medical Research Council [MC_U105170645] Funding Source: researchfish
Proton-translocating ATPases are ubiquitous protein complexes that couple ATP catalysis with proton translocation via a rotary catalytic mechanism. The peripheral stalks are essential components that counteract torque generated from proton translocation during ATP synthesis or from ATP hydrolysis during proton pumping. Despite their essential role, the peripheral stalks are the least conserved component of the complexes, differing substantially between subtypes in composition and stoichiometry. We have determined the crystal structure of the peripheral stalk of the A-type ATPase/synthase from Thermus thermophilus consisting of subunits E and G. The structure contains a heterodimeric right-handed coiled coil, a protein fold never observed before. We have fitted this structure into the 23 angstrom resolution EM density of the intact A-ATPase complex, revealing the precise location of the peripheral stalk and new implications for the function and assembly of proton-translocating ATPases.
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