2WIE

High-resolution structure of the rotor ring from a proton dependent ATP synthase

Summary for 2WIE

• Entry DOI: 10.2210/pdb2wie/pdb
• Descriptor: ATP SYNTHASE C CHAIN, CYMAL-4 (3 entities in total)
• Functional Keywords: hydrolase, f1fo atp synthase rotor, ion proton-translocation, ion transport, transmembrane, c-ring structure, spirulina platensis, hydrogen ion transport, membrane protein complex, cf(0), membrane, lipid-binding
• Biological source: ARTHROSPIRA PLATENSIS
• Total number of polymer chains: 5
• Total formula weight: 60279.49

Authors

Pogoryelov, D.,Yildiz, O.,Faraldo-Gomez, J.D.,Meier, T. (deposition date: 2009-05-11, release date: 2009-09-29, Last modification date: 2024-11-20)

Primary citation

Pogoryelov, D.,Yildiz, O.,Faraldo-Gomez, J.D.,Meier, T.
High-Resolution Structure of the Rotor Ring of a Proton-Dependent ATP Synthase.
Nat.Struct.Mol.Biol., 16:1068-, 2009

PubMed Abstract: The crystal structure of the c-ring from the proton-coupled F1Fo ATP synthase from Spirulina platensis is shown at 2.1-A resolution. The ring includes 15 membrane-embedded c subunits forming an hourglass-shaped assembly. The structure demonstrates that proton translocation across the membrane entails protonation of a conserved glutamate located near the membrane center in the c subunit outer helix. The proton is locked in this site by a precise hydrogen bond network reminiscent of that in Na+-dependent ATP synthases. However, the structure suggests that the different coordination chemistry of the bound proton and the smaller curvature of the outer helix drastically enhance the selectivity of the H+ site against other cations, including H3O+. We propose a model for proton translocation whereby the c subunits remain in this proton-locked state when facing the membrane lipid. Proton exchange would occur in a more hydrophilic and electrostatically distinct environment upon contact with the a subunit interface.

PubMed: 19783985
DOI: 10.1038/NSMB.1678

Experimental method

X-RAY DIFFRACTION (2.13 Å)