5T4O

Autoinhibited E. coli ATP synthase state 1

Summary for 5T4O

• Entry DOI: 10.2210/pdb5t4o/pdb
• Related: 5T4P 5T4Q
• EMDB information: 8357 8358 8359
• Descriptor: ATP synthase subunit alpha, ADENOSINE-5'-DIPHOSPHATE, ATP synthase subunit beta, ... (10 entities in total)
• Functional Keywords: atp synthase, atpase, rotary motor, membrane protein, hydrolase
• Biological source: Escherichia coli; More
• Cellular location: Cell inner membrane ; Peripheral membrane protein : B7MGF4 B7MGF2 B7MGF3 B7MGF1 B7MGF5; Cell inner membrane ; Single-pass membrane protein : P0ABA2; Cell inner membrane ; Multi-pass membrane protein : B7L888 B7NR39
• Total number of polymer chains: 22
• Total formula weight: 535441.77

Authors

Sobti, M.,Smits, C.,Wong, A.S.W.,Ishmukhametov, R.,Stock, D.,Sandin, S.,Stewart, A.G. (deposition date: 2016-08-29, release date: 2016-12-28, Last modification date: 2024-03-13)

Primary citation

Sobti, M.,Smits, C.,Wong, A.S.,Ishmukhametov, R.,Stock, D.,Sandin, S.,Stewart, A.G.
Cryo-EM structures of the autoinhibitedE. coliATP synthase in three rotational states.
Elife, 5:-, 2016

PubMed Abstract: A molecular model that provides a framework for interpreting the wealth of functional information obtained on the F-ATP synthase has been generated using cryo-electron microscopy. Three different states that relate to rotation of the enzyme were observed, with the central stalk's ε subunit in an extended autoinhibitory conformation in all three states. The F motor comprises of seven transmembrane helices and a decameric c-ring and invaginations on either side of the membrane indicate the entry and exit channels for protons. The proton translocating subunit contains near parallel helices inclined by ~30° to the membrane, a feature now synonymous with rotary ATPases. For the first time in this rotary ATPase subtype, the peripheral stalk is resolved over its entire length of the complex, revealing the F attachment points and a coiled-coil that bifurcates toward the membrane with its helices separating to embrace subunit from two sides.

PubMed: 28001127
DOI: 10.7554/eLife.21598

Experimental method

ELECTRON MICROSCOPY (6.9 Å)