The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase

Journal Article · Mon Mar 22 04:00:00 EDT 2010 · Nat. Struct. Mol. Biol.

DOI:https://doi.org/10.1038/nsmb.1761· OSTI ID:1002303

Lee, Lawrence K; Stewart, Alastair G; Donohoe, Mhairi; Bernal, Ricardo A; Stock, Daniela ^[1]

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1. VCCRI

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.

• Research Organization: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
• Sponsoring Organization: USDOE
• OSTI ID: 1002303
• Journal Information: Nat. Struct. Mol. Biol., Journal Name: Nat. Struct. Mol. Biol. Journal Issue: (3) ; 03, 2010 Vol. 17; ISSN 1545-9985; ISSN 1545-9993
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

36 MATERIALS SCIENCE
CATALYSIS
CRYSTAL STRUCTURE
HYDROLYSIS
PROTEINS
PROTONS
PUMPING
RESOLUTION
STOICHIOMETRY
SYNTHESIS
TORQUE
TRANSLOCATION