1AQT

EPSILON SUBUNIT OF F1F0-ATP SYNTHASE FROM ESCHERICHIA COLI

Summary for 1AQT

• Entry DOI: 10.2210/pdb1aqt/pdb
• Descriptor: ATP SYNTHASE (2 entities in total)
• Functional Keywords: hydrolase, atpase, atp synthase, epsilon subunit
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 14897.90

Authors

Uhlin, U.,Guss, J.M. (deposition date: 1997-07-31, release date: 1998-02-04, Last modification date: 2024-02-07)

Primary citation

Uhlin, U.,Cox, G.B.,Guss, J.M.
Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli.
Structure, 5:1219-1230, 1997

PubMed Abstract: Proton-translocating ATP synthases convert the energy generated from photosynthesis or respiration into ATP. These enzymes, termed F0F1-ATPases, are structurally highly conserved. In Escherichia coli, F0F1-ATPase consists of a membrane portion, F0, made up of three different polypeptides (a, b and c) and an F1 portion comprising five different polypeptides in the stoichiometry alpha 3 beta 3 gamma delta epsilon. The minor subunits gamma, delta and epsilon are required for the coupling of proton translocation with ATP synthesis; the epsilon subunit is in close contact with the alpha, beta, gamma and c subunits. The structure of the epsilon subunit provides clues to its essential role in this complex enzyme.

PubMed: 9331422
DOI: 10.1016/S0969-2126(97)00272-4

Experimental method

X-RAY DIFFRACTION (2.3 Å)