Stairway to translocation: AAA+ motor structures reveal the mechanisms of ATP-dependent substrate translocation.

ABSTRACT: Translocases of the AAA+ (ATPases Associated with various cellular Activities) family are powerful molecular machines that use the mechano-chemical coupling of ATP hydrolysis and conformational changes to thread DNA or protein substrates through their central channel for many important biological processes. These motors comprise hexameric rings of ATPase subunits, in which highly conserved nucleotide-binding domains form active-site pockets near the subunit interfaces and aromatic pore-loop residues extend into the central channel for substrate binding and mechanical pulling. Over the past 2 years, 41 cryo-EM structures have been solved for substrate-bound AAA+ translocases that revealed spiral-staircase arrangements of pore-loop residues surrounding substrate polypeptides and indicating a

SUBMITTER: Gates SN 

PROVIDER: S-EPMC6954725 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature