6OQR

E. coli ATP Synthase ADP State 1a

Summary for 6OQR

• Entry DOI: 10.2210/pdb6oqr/pdb
• EMDB information: 20167
• Descriptor: ATP synthase subunit delta, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (12 entities in total)
• Functional Keywords: e coli atp synthase, ion channel, atpase, membrane protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 22
• Total formula weight: 537269.21

Authors

Stewart, A.G.,Walshe, J.L.,Sobti, M. (deposition date: 2019-04-29, release date: 2020-06-03, Last modification date: 2024-03-20)

Primary citation

Sobti, M.,Walshe, J.L.,Wu, D.,Ishmukhametov, R.,Zeng, Y.C.,Robinson, C.V.,Berry, R.M.,Stewart, A.G.
Cryo-EM structures provide insight into how E. coli F1FoATP synthase accommodates symmetry mismatch.
Nat Commun, 11:2615-2615, 2020

PubMed Abstract: FF 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 motor generates rotation of the central stalk, inducing conformational changes in the F 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 associated with long-range conformational changes that indicates how this flexibility accommodates the mismatch between the 3- and 10-fold symmetries of the F and F motors. We also identify density likely corresponding to lipid molecules that may contribute to the rotor/stator interaction within the F motor.

PubMed: 32457314
DOI: 10.1038/s41467-020-16387-2

Experimental method

ELECTRON MICROSCOPY (3.1 Å)