Insights into FlaI functions in archaeal motor assembly and motility from structures, conformations, and genetics.

Insights into FlaI functions in archaeal motor assembly and motility from structures, conformations, and genetics.
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DOI:
10.1016/j.molcel.2013.01.014
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发表时间:
2013-03-28
期刊:
影响因子:
16
通讯作者:
Tainer, John A.
Tainer, John A.
中科院分区:
生物学1区
文献类型:
--
作者:
Reindl, Sophia;Ghosh, Abhrajyoti;Williams, Gareth J.;Lassak, Kerstin;Neiner, Tomasz;Henche, Anna-Lena;Albers, Sonja-Verena;Tainer, John A.

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Superfamily ATPases in Type IV pili (T4P), Type 2 secretion (T2S), and archaella (formerly archaeal flagella) employ similar sequences for distinct biological processes. Here we structurally and functionally characterize prototypical superfamily ATPase FlaI from Sulfolobus acidocaldarius showing FlaI activities in archaeal swimming organelle assembly and movement. FlaI solution X-ray scattering 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 distinctly from secretion and pilus ATPases. Crown interactions and conformations regulate assembly, motility and force direction by 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.
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