The mechanism and energetics of the dynein priming stroke

Mert Golcuk, Sema Zeynep Yilmaz, Ahmet Yildiz, Mert Gur*

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Özet

Dyneins are an AAA+ motor responsible for motility and force generation toward the minus end of microtubules. Dynein motility is powered by nucleotide-dependent transitions of its linker domain, which transitions between straight (post-powerstroke) and bent (pre-powerstroke) conformations. To understand the dynamics and energetics of the linker, we performed all-atom molecular dynamics simulations of human dynein-2 primed for its power stroke. Simulations revealed that the linker can adopt either a bent conformation or a semi-bent conformation, separated by a 5.7 kT energy barrier. The linker cannot switch back to its straight conformation in the pre-powerstroke state due to a steric clash with the AAA+ ring. Simulations also showed that an isolated linker has a free energy minimum near the semi-bent conformation in the absence of the AAA+ ring, indicating that the linker stores energy as it bends and releases this energy during the powerstroke.

Orijinal dilİngilizce
Sayfa (başlangıç-bitiş)603-610.e4
DergiStructure
Hacim32
Basın numarası5
DOI'lar
Yayın durumuYayınlandı - 2 May 2024

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© 2024 Elsevier Ltd

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