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|3oaa, resolution 3.26Å ()|
|Ligands:||, , ,|
|Gene:||atpA, EcDH1_4233 (Escherichia coli DH1), atpD, EcDH1_4235 (Escherichia coli DH1), EcDH1_4234 (Escherichia coli DH1), atpC, EcDH1_4236 (Escherichia coli DH1)|
Structure of the E.coli F1-ATP synthase inhibited by subunit Epsilon
ATP synthase is a membrane-bound rotary motor enzyme that is critical for cellular energy metabolism in all kingdoms of life. Despite conservation of its basic structure and function, autoinhibition by one of its rotary stalk subunits occurs in bacteria and chloroplasts but not in mitochondria. The crystal structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli described here reveals the structural basis for this inhibition. The C-terminal domain of subunit varepsilon adopts a heretofore unknown, highly extended conformation that inserts deeply into the central cavity of the enzyme and engages both rotor and stator subunits in extensive contacts that are incompatible with functional rotation. As a result, the three catalytic subunits are stabilized in a set of conformations and rotational positions distinct from previous F(1) structures.
Structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli in an autoinhibited conformation., Cingolani G, Duncan TM, Nat Struct Mol Biol. 2011 Jun;18(6):701-7. Epub 2011 May 22. PMID:021602818
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.