Abstract：
:Membrane-bound pyrophosphatases (M-PPases), which couple proton/sodium ion transport to pyrophosphate synthesis/hydrolysis, are important in abiotic stress resistance and in the infectivity of protozoan parasites. Here, three M-PPase structures in different catalytic states show that closure of the substrate-binding pocket by helices 5-6 affects helix 13 in the dimer interface and causes helix 12 to move down. This springs a 'molecular mousetrap', repositioning a conserved aspartate and activating the nucleophilic water. Corkscrew motion at helices 6 and 16 rearranges the key ionic gate residues and leads to ion pumping. The pumped ion is above the ion gate in one of the ion-bound structures, but below it in the other. Electrometric measurements show a single-turnover event with a non-hydrolysable inhibitor, supporting our model that ion pumping precedes hydrolysis. We propose a complete catalytic cycle for both proton and sodium-pumping M-PPases, and one that also explains the basis for ion specificity.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Li KM,Wilkinson C,Kellosalo J,Tsai JY,Kajander T,Jeuken LJ,Sun YJ,Goldman Adoi
10.1038/ncomms13596subject
Has Abstractpub_date
2016-12-06 00:00:00pages
13596issn
2041-1723pii
ncomms13596journal_volume
7pub_type
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