The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution.

TitleThe structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution.
Publication TypeJournal Article
Year of Publication2000
AuthorsGibbons, C, Montgomery, MG, Leslie, AG, Walker, JE
JournalNat Struct Biol
Date Published2000 Nov
KeywordsAnimals, Binding Sites, Catalysis, Catalytic Domain, Cattle, Crystallization, Crystallography, X-Ray, Dicyclohexylcarbodiimide, Macromolecular Substances, Mitochondria, Models, Molecular, Protein Binding, Protein Structure, Quaternary, Protein Structure, Secondary, Protein Subunits, Proton-Motive Force, Proton-Translocating ATPases, Rotation, Structure-Activity Relationship

The central stalk in ATP synthase, made of gamma, delta and epsilon subunits in the mitochondrial enzyme, is the key rotary element in the enzyme's catalytic mechanism. The gamma subunit penetrates the catalytic (alpha beta)(3) domain and protrudes beneath it, interacting with a ring of c subunits in the membrane that drives rotation of the stalk during ATP synthesis. In other crystals of F(1)-ATPase, the protrusion was disordered, but with crystals of F(1)-ATPase inhibited with dicyclohexylcarbodiimide, the complete structure was revealed. The delta and epsilon subunits interact with a Rossmann fold in the gamma subunit, forming a foot. In ATP synthase, this foot interacts with the c-ring and couples the transmembrane proton motive force to catalysis in the (alpha beta)(3) domain.

Alternate JournalNat. Struct. Biol.
Citation Key10.1038/80981
PubMed ID11062563