Structure of the ATP synthase catalytic complex (F1) from Escherichia coli in an auto-inhibited conformation

  title={Structure of the ATP synthase catalytic complex (F1) from Escherichia coli in an auto-inhibited conformation},
  author={Gino Cingolani and Thomas M. Duncan},
  journal={Nature structural \& molecular biology},
  pages={701 - 707}
ATP synthase is a membrane-bound rotary motor enzyme that is critical for cellular energy metabolism in all kingdoms of life. Despite conservation of its basic structure and function, autoinhibition by one of its rotary stalk subunits occurs in bacteria and chloroplasts but not in mitochondria. The crystal structure of the ATP synthase catalytic complex (F1) from Escherichia coli described here reveals the structural basis for this inhibition. The C-terminal domain of subunit ɛ adopts a… 

Structure of a bacterial ATP synthase

The architecture of the membrane region shows how the simple bacterial ATP synthase is able to perform the same core functions as the equivalent, but more complicated, mitochondrial complex, and reveals the path of transmembrane proton translocation.

The regulatory subunit ε in Escherichia coli FOF1-ATP synthase.

F1-ATPase of Escherichia coli

The rapid effects of catalytic site ligands on conformational changes of F1-bound ϵ suggest dynamic conformational and rotational mobility in F1 that is paused near the catalytic dwell position, and ϵ inhibition may provide a new target for antimicrobial discovery.

Conformational dynamics of the rotary subunit F in the A3B3DF complex of Methanosarcina mazei Gö1 A‐ATP synthase monitored by single‐molecule FRET

This work investigated the nucleotide‐dependent conformational changes of subunit F relative to subunit D during ATP hydrolysis in the A3B3DF complex of the Methanosarcina mazei Gö1 A‐ATP synthase using single‐molecule Förster resonance energy transfer and found two conformations.

A Conformational Change of the γ Subunit Indirectly Regulates the Activity of Cyanobacterial F1-ATPase*

The results imply that the global conformational change of the γ subunit indirectly regulates complex activity by changing both ADP inhibition and ϵ inhibition.

The N-terminal region of the ϵ subunit from cyanobacterial ATP synthase alone can inhibit ATPase activity

ATP hydrolysis activity catalyzed by chloroplast and proteobacterial ATP synthase is inhibited by their ϵ subunits. To clarify the function of the ϵ subunit from phototrophs, here we analyzed the ϵ

Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data

It is concluded that the ɛ subunit from the bacterial F-type ATP synthases is indeed capable of regulating ATP hydrolysis activity in a wide variety of bacteria, making it a potentially valuable drug target, but its exact role is still under debate.

Analysis of an N-terminal deletion in subunit a of the Escherichia coli ATP synthase

Results indicate that loss of the N-terminal region of subunit a does not generally disrupt its structure, but does alter interactions with subunit b, which is essential for proton translocation.



The structure of the central stalk in bovine F1-ATPase at 2.4 Å resolution

The central stalk in ATP synthase is made of γ, δ and ɛ subunits in the mitochondrial enzyme, and with crystals of F1-ATPase inhibited with dicyclohexylcarbodiimide, the complete structure was revealed.

Structures of the thermophilic F1-ATPase ε subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1

It is suggested that the ε C-terminal domain can undergo an arm-like motion in response to an ATP concentration change and thereby contribute to regulation of FoF1-ATP synthase.

Structure of the γ–ɛ complex of ATP synthase

ATP synthases (F1Fo-ATPases) use energy released by the movement of protons down a transmembrane electrochemical gradient to drive the synthesis of ATP, the universal biological energy currency.

Asymmetric Structure of the Yeast F1 ATPase in the Absence of Bound Nucleotides*

The crystal structure of nucleotide-free yeast F1 ATPase has been determined and the adenine-binding pocket of the βTP subunits is disrupted in the apoenzyme, suggesting that the βDP subunit is responsible for unisite catalytic activity.

Rotor/Stator Interactions of the ϵ Subunit in Escherichia coli ATP Synthase and Implications for Enzyme Regulation*

Disulfide cross-linking of substituted cysteines on functionally coupled ATP synthase is used to characterize interactions of ϵ with an F0 component of the rotor (subunit c) and with an C-terminal domain of the stator ( subunit β) to demonstrate the ability ofπ to span the central stalk region from the surface of the membrane (ϵ-c) to the bottom of F1 (β-ϵ).

The ATP synthase--a splendid molecular machine.

  • P. Boyer
  • Chemistry
    Annual review of biochemistry
  • 1997
An X-ray structure of the F1 portion of the mitochondrial ATP synthase shows asymmetry and differences in nucleotide binding of the catalytic beta subunits that support the binding change mechanism

Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase

The shifts in position of the central stalk between two of the three copies of yeast F1 ATPase give new insight into the conformational changes that take place during rotational catalysis.

Rotation of subunits during catalysis by Escherichia coli F1-ATPase.

The results demonstrate that gamma subunit rotates relative to the beta subunits during catalysis, and similar reactivities of unlabeled and radiolabeled beta sub units with gamma C87 upon reoxidation.