PDBsum entry 6oqw

Membrane protein

PDB id: 6oqw

Contents

Protein chains

173 a.a.

510 a.a.

153 a.a.

136 a.a.

284 a.a.

458 a.a.

(+ 4 more) 77 a.a.

266 a.a.

Ligands

ATP ×3

ADP ×3

PO4

Metals

_MG ×5

References listed in PDB file

Key reference

• Title: Cryo-Em structures provide insight into how e. Coli f₁f_o ATP synthase accommodates symmetry mismatch.
• Authors: M.Sobti, J.L.Walshe, D.Wu, R.Ishmukhametov, Y.C.Zeng, C.V.Robinson, R.M.Berry, A.G.Stewart.
• Ref.: Nat Commun, 2020, 11, 2615. [DOI no: 10.1038/s41467-020-16387-2]
• PubMed id: 32457314

Abstract

F₁F_o ATP synthase functions as a biological rotary generator that makes a major contribution to cellular energy production. It comprises two molecular motors coupled together by a central and a peripheral stalk. Proton flow through the F_o motor generates rotation of the central stalk, inducing conformational changes in the F₁ motor that catalyzes ATP production. Here we present nine cryo-EM structures of E. coli ATP synthase to 3.1-3.4 Å resolution, in four discrete rotational sub-states, which provide a comprehensive structural model for this widely studied bacterial molecular machine. We observe torsional flexing of the entire complex and a rotational sub-step of F_o associated with long-range conformational changes that indicates how this flexibility accommodates the mismatch between the 3- and 10-fold symmetries of the F₁ and F_o motors. We also identify density likely corresponding to lipid molecules that may contribute to the rotor/stator interaction within the F_o motor.