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Conformational dynamics of the rotary subunit F in the A 3 B 3 DF complex of Methanosarcina mazei Gö1 A‐ ATP synthase monitored by single‐molecule FRET
Author(s) -
Singh Dhirendra,
Sielaff Hendrik,
Börsch Michael,
Grüber Gerhard
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12605
Subject(s) - atp synthase gamma subunit , atp hydrolysis , atp synthase , protein subunit , conformational change , chemistry , atpase , transmembrane domain , cyclic nucleotide binding domain , stereochemistry , adenosine triphosphate , biochemistry , nucleotide , biophysics , crystallography , biology , enzyme , membrane , gene
In archaea the A 1 A O ATP synthase uses a transmembrane electrochemical potential to generate ATP , while the soluble A 1 domain (subunits A 3 B 3 DF ) alone can hydrolyse ATP . The three nucleotide‐binding AB pairs form a barrel‐like structure with a central orifice that hosts the rotating central stalk subunits DF. ATP binding, hydrolysis and product release cause a conformational change inside the A:B‐interface, which enforces the rotation of subunits DF. Recently, we reported that subunit F is a stimulator of ATP ase activity. Here, we investigated the nucleotide‐dependent conformational changes of subunit F relative to subunit D during ATP hydrolysis in the A 3 B 3 DF complex of the Methanosarcina mazei Gö1 A‐ ATP synthase using single‐molecule Förster resonance energy transfer. We found two conformations for subunit F during ATP hydrolysis.