Structure of a catalytic dimer of the α- and β-subunits of the F-ATPase from Paracoccus denitrificans at 2.3 Å resolution

Morales-Ríos, E.; Montgomery, M.G.; Leslie, A.G.W.; García-Trejo, J.J.; Walker, J.E.

doi:10.1107/S2053230X15016076

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 3
Structure of the catalytic dimer of the α- and β-subunits of the F-ATPase from P. denitrificans. The α- and β-subunits are shown in red and yellow, respectively, and a bound phosphate ion is denoted by cyan spheres. (a) View from the front, looking inwards towards the central stalk in the rotor of the intact enzyme. The arrangement of subunits, with the α-subunit on the left and the β-subunit on the right, corresponds to a catalytic interface in the intact F₁-ATPase. (b) View from the inside of the intact complex, looking outwards.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 71| Part 10| September 2015| Pages 1309-1317

doi:10.1107/S2053230X15016076

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