Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Cryo-EM structures provide insight into how E. coli FF ATP synthase accommodates symmetry mismatch.
Journal, issue, pages	Nat Commun, Vol. 11, Issue 1, Page 2615, Year 2020
Publish date	May 26, 2020
Authors	Meghna Sobti / James L Walshe / Di Wu / Robert Ishmukhametov / Yi C Zeng / Carol V Robinson / Richard M Berry / Alastair G Stewart /
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 ...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.
External links	Nat Commun / PubMed:32457314 / PubMed Central
Methods	EM (single particle)
Resolution	3.1 - 3.4 Å
Structure data	20167 6oqr EMDB-20167, PDB-6oqr: E. coli ATP Synthase ADP State 1a Method: EM (single particle) / Resolution: 3.1 Å 20168 6oqs EMDB-20168, PDB-6oqs: E. coli ATP synthase State 1b Method: EM (single particle) / Resolution: 3.3 Å 20169 6oqt EMDB-20169, PDB-6oqt: E. coli ATP synthase State 1c Method: EM (single particle) / Resolution: 3.1 Å 20170 6oqu EMDB-20170, PDB-6oqu: E. coli ATP synthase State 1d Method: EM (single particle) / Resolution: 3.2 Å 20171 6oqv EMDB-20171, PDB-6oqv: E. coli ATP Synthase State 2b Method: EM (single particle) / Resolution: 3.3 Å 20172 6oqw EMDB-20172, PDB-6oqw: E. coli ATP synthase State 3a Method: EM (single particle) / Resolution: 3.1 Å 20454 6pqv EMDB-20454, PDB-6pqv: E. coli ATP Synthase State 1e Method: EM (single particle) / Resolution: 3.3 Å 21419 6vwk EMDB-21419, PDB-6vwk: E. coli ATP Synthase ADP Sub-state 3a Fo Focussed Method: EM (single particle) / Resolution: 3.3 Å 21854 6wnq EMDB-21854, PDB-6wnq: E. coli ATP Synthase State 2a Method: EM (single particle) / Resolution: 3.4 Å 21855 6wnr EMDB-21855, PDB-6wnr: E. coli ATP synthase State 3b Method: EM (single particle) / Resolution: 3.3 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-MG: Unknown entry ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-PO4: PHOSPHATE ION
Source	escherichia coli (E. coli) Escherichia coli escherichia coli 2-427-07_s4_c3 (bacteria) escherichia coli o145:nm (bacteria) escherichia coli chi7122 (bacteria) escherichia coli xuzhou21 (bacteria)
Keywords	MEMBRANE PROTEIN / E coli ATP Synthase / ion channel / ATPase / F1Fo ATP synthase