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Instruments / Technical Area	Publication Details	Published
I02-Macromolecular Crystallography	How release of phosphate from mammalian F\|1\|-ATPase generates a rotary substep. John Bason , Martin Montgomery , Andrew Leslie , John E. Walker Proceedings Of The National Academy Of Sciences 112 (19), 6009 - 6014 DOI: 10.1073/pnas.1506465112 PMID: 25918412 Diamond Proposal Number(s): [6641, 8547] Open Access Show Abstract ▼ Abstract: The rotation of the central stalk of F1-ATPase is driven by energy derived from the sequential binding of an ATP molecule to its three catalytic sites and the release of the products of hydrolysis. In human F1-ATPase, each 360° rotation consists of three 120° steps composed of substeps of about 65°, 25°, and 30°, with intervening ATP binding, phosphate release, and catalytic dwells, respectively. The F1-ATPase inhibitor protein, IF1, halts the rotary cycle at the catalytic dwell. The human and bovine enzymes are essentially identical, and the structure of bovine F1-ATPase inhibited by IF1 represents the catalytic dwell state. Another structure, described here, of bovine F1-ATPase inhibited by an ATP analog and the phosphate analog, thiophosphate, represents the phosphate binding dwell. Thiophosphate is bound to a site in the Alpha (E) Beta (E)-catalytic interface, whereas in F1-ATPase inhibited with IF1, the equivalent site is changed subtly and the enzyme is incapable of binding thiophosphate. These two structures provide a molecular mechanism of how phosphate release generates a rotary substep as follows. In the active enzyme, phosphate release from the Beta (E)-subunit is accompanied by a rearrangement of the structure of its binding site that prevents released phosphate from rebinding. The associated extrusion of a loop in the beta (E)-subunit disrupts interactions in the Alpha (E) Beta (E)-catalytic interface and opens it to its fullest extent. Other rearrangements disrupt interactions between the Gamma-subunit and the C-terminal domain of the Alpha (E)-subunit. To restore most of these interactions, and to make compensatory new ones, the Gamma-subunit rotates through 25°-30°.	May 2015
I04-1-Macromolecular Crystallography (fixed wavelength)	Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution Edgar Morales-rios , Martin Montgomery , Andrew Leslie , John E. Walker Proceedings Of The National Academy Of Sciences DOI: 10.1073/pnas.1517542112 PMID: 26460036 Diamond Proposal Number(s): [26460036] Show Abstract ▼ Abstract: The structure of the intact ATP synthase from the α-proteobacterium Paracoccus denitrificans, inhibited by its natural regulatory ζ-protein, has been solved by X-ray crystallography at 4.0 Å resolution. The ζ-protein is bound via its N-terminal α-helix in a catalytic interface in the F1 domain. The bacterial F1 domain is attached to the membrane domain by peripheral and central stalks. The δ-subunit component of the peripheral stalk binds to the N-terminal regions of two α-subunits. The stalk extends via two parallel long α-helices, one in each of the related b and b′ subunits, down a noncatalytic interface of the F1 domain and interacts in an unspecified way with the a-subunit in the membrane domain. The a-subunit lies close to a ring of 12 c-subunits attached to the central stalk in the F1 domain, and, together, the central stalk and c-ring form the enzyme’s rotor. Rotation is driven by the transmembrane proton-motive force, by a mechanism where protons pass through the interface between the a-subunit and c-ring via two half-channels in the a-subunit. These half-channels are probably located in a bundle of four α-helices in the a-subunit that are tilted at ∼30° to the plane of the membrane. Conserved polar residues in the two α-helices closest to the c-ring probably line the proton inlet path to an essential carboxyl group in the c-subunit in the proton uptake site and a proton exit path from the proton release site. The structure has provided deep insights into the workings of this extraordinary molecular machine.	Oct 2015
Krios I-Titan Krios I at Diamond Krios II-Titan Krios II at Diamond Krios III-Titan Krios III at Diamond Krios IV-Titan Krios IV at Diamond	Structure of the dimeric ATP synthase from bovine mitochondria Tobias E. Spikes , Martin Montgomery , John E. Walker Proceedings Of The National Academy Of Sciences 117, 23519 - 23526 DOI: 10.1073/pnas.2013998117 Diamond Proposal Number(s): [13954, 17057, 16422, 18075] Open Access Show Abstract ▼ Abstract: The structure of the dimeric ATP synthase from bovine mitochondria determined in three rotational states by electron cryo-microscopy provides evidence that the proton uptake from the mitochondrial matrix via the proton inlet half channel proceeds via a Grotthus mechanism, and a similar mechanism may operate in the exit half channel. The structure has given information about the architecture and mechanical constitution and properties of the peripheral stalk, part of the membrane extrinsic region of the stator, and how the action of the peripheral stalk damps the side-to-side rocking motions that occur in the enzyme complex during the catalytic cycle. It also describes wedge structures in the membrane domains of each monomer, where the skeleton of each wedge is provided by three α-helices in the membrane domains of the b-subunit to which the supernumerary subunits e, f, and g and the membrane domain of subunit A6L are bound. Protein voids in the wedge are filled by three specifically bound cardiolipin molecules and two other phospholipids. The external surfaces of the wedges link the monomeric complexes together into the dimeric structures and provide a pivot to allow the monomer–monomer interfaces to change during catalysis and to accommodate other changes not related directly to catalysis in the monomer–monomer interface that occur in mitochondrial cristae. The structure of the bovine dimer also demonstrates that the structures of dimeric ATP synthases in a tetrameric porcine enzyme have been seriously misinterpreted in the membrane domains.	Sep 2020

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