Abstract:
:Superfamily ATPases in type IV pili, type 2 secretion, and archaella (formerly archaeal flagella) employ similar sequences for distinct biological processes. Here, we structurally and functionally characterize prototypical superfamily ATPase FlaI in Sulfolobus acidocaldarius, showing FlaI activities in archaeal swimming-organelle assembly and movement. X-ray scattering data of FlaI in solution and crystal structures with and without nucleotide reveal a hexameric crown assembly with key cross-subunit interactions. Rigid building blocks form between N-terminal domains (points) and neighboring subunit C-terminal domains (crown ring). Upon nucleotide binding, these six cross-subunit blocks move with respect to each other and distinctly from secretion and pilus ATPases. Crown interactions and conformations regulate assembly, motility, and force direction via a basic-clamp switching mechanism driving conformational changes between stable, backbone-interconnected moving blocks. Collective structural and mutational results identify in vivo functional components for assembly and motility, phosphate-triggered rearrangements by ATP hydrolysis, and molecular predictors for distinct ATPase superfamily functions.
journal_name
Mol Celljournal_title
Molecular cellauthors
Reindl S,Ghosh A,Williams GJ,Lassak K,Neiner T,Henche AL,Albers SV,Tainer JAdoi
10.1016/j.molcel.2013.01.014subject
Has Abstractpub_date
2013-03-28 00:00:00pages
1069-82issue
6eissn
1097-2765issn
1097-4164pii
S1097-2765(13)00047-6journal_volume
49pub_type
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