2XQT
Microscopic rotary mechanism of ion translocation in the Fo complex of ATP synthases
Summary for 2XQT
| Entry DOI | 10.2210/pdb2xqt/pdb |
| Related | 2XQS 2XQU |
| Descriptor | ATP SYNTHASE C CHAIN, DICYCLOHEXYLUREA, CYMAL-4, ... (4 entities in total) |
| Functional Keywords | membrane protein, f1fo-atp synthase rotor, c-ring, ion (proton, h+)-translocation, n\, n'- dicyclohexylcarbodiimide (dccd) inhibitor |
| Biological source | ARTHROSPIRA PLATENSIS |
| Total number of polymer chains | 5 |
| Total formula weight | 63803.93 |
| Authors | Pogoryelov, D.,Krah, A.,Langer, J.,Yildiz, O.,Faraldo-Gomez, J.D.,Meier, T. (deposition date: 2010-09-07, release date: 2010-10-27, Last modification date: 2024-10-09) |
| Primary citation | Pogoryelov, D.,Krah, A.,Langer, J.,Yildiz, O.,Faraldo-Gomez, J.D.,Meier, T. Microscopic Rotary Mechanism of Ion Translocation in the Fo Complex of ATP Synthases Nat.Chem.Biol., 6:891-, 2010 Cited by PubMed Abstract: The microscopic mechanism of coupled c-ring rotation and ion translocation in F(1)F(o)-ATP synthases is unknown. Here we present conclusive evidence supporting the notion that the ability of c-rings to rotate within the F(o) complex derives from the interplay between the ion-binding sites and their nonhomogenous microenvironment. This evidence rests on three atomic structures of the c(15) rotor from crystals grown at low pH, soaked at high pH and, after N,N'-dicyclohexylcarbodiimide (DCCD) modification, resolved at 1.8, 3.0 and 2.2 Å, respectively. Alongside a quantitative DCCD-labeling assay and free-energy molecular dynamics calculations, these data demonstrate how the thermodynamic stability of the so-called proton-locked state is maximized by the lipid membrane. By contrast, a hydrophilic environment at the a-subunit-c-ring interface appears to unlock the binding-site conformation and promotes proton exchange with the surrounding solution. Rotation thus occurs as c-subunits stochastically alternate between these environments, directionally biased by the electrochemical transmembrane gradient. PubMed: 20972431DOI: 10.1038/NCHEMBIO.457 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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