In situstructure and rotary states of mitochondrial ATP synthase in whole cells

Author:

Dietrich LeaORCID,Agip Ahmed-Noor AdamORCID,Schwarz AndreORCID,Kunz Christina,Kühlbrandt WernerORCID

Abstract

ABSTRACTCells depend on a continuous supply of ATP, the universal energy currency. In mitochondria, ATP is produced by a series of redox reactions, whereby an electrochemical gradient is established across the inner mitochondrial membrane. The ATP synthase harnesses the energy of the gradient to generate ATP from ADP and inorganic phosphate. We determined the structure of ATP synthase within mitochondria of the unicellular algaPolytomellaby electron cryo-tomography. Sub-tomogram averaging revealed six rotary positions of the central stalk, subclassified into 21 substates of the F1head. ThePolytomellaATP synthase forms helical arrays with multiple adjacent rows defining the cristae ridges. The structure of ATP synthase under native operating conditions in the presence of a membrane potential represents a pivotal step toward the analysis of membrane protein complexesin situ.

Publisher

Cold Spring Harbor Laboratory

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