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TitleStructural basis for two-way communication between dynein and microtubules.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 1038, Year 2020
Publish dateFeb 25, 2020
AuthorsNoritaka Nishida / Yuta Komori / Osamu Takarada / Atsushi Watanabe / Satoko Tamura / Satoshi Kubo / Ichio Shimada / Masahide Kikkawa /
PubMed AbstractThe movements of cytoplasmic dynein on microtubule (MT) tracks is achieved by two-way communication between the microtubule-binding domain (MTBD) and the ATPase domain via a coiled-coil stalk, but ...The movements of cytoplasmic dynein on microtubule (MT) tracks is achieved by two-way communication between the microtubule-binding domain (MTBD) and the ATPase domain via a coiled-coil stalk, but the structural basis of this communication remains elusive. Here, we regulate MTBD either in high-affinity or low-affinity states by introducing a disulfide bond to the stalk and analyze the resulting structures by NMR and cryo-EM. In the MT-unbound state, the affinity changes of MTBD are achieved by sliding of the stalk α-helix by a half-turn, which suggests that structural changes propagate from the ATPase-domain to MTBD. In addition, MT binding induces further sliding of the stalk α-helix even without the disulfide bond, suggesting how the MT-induced conformational changes propagate toward the ATPase domain. Based on differences in the MT-binding surface between the high- and low-affinity states, we propose a potential mechanism for the directional bias of dynein movement on MT tracks.
External linksNat Commun / PubMed:32098965 / PubMed Central
MethodsEM (helical sym.) / NMR (solution)
Resolution3.62 - 3.94 Å
Structure data

9996

6kio

EMDB-9996, PDB-6kio:
Complex of yeast cytoplasmic dynein MTBD-High and MT without DTT
Method: EM (helical sym.) / Resolution: 3.94 Å

9997

6kiq

EMDB-9997, PDB-6kiq:
Complex of yeast cytoplasmic dynein MTBD-High and MT with DTT
Method: EM (helical sym.) / Resolution: 3.62 Å

PDB-6kjn:
The microtubule-binding domains of yeast cytoplasmic dynein in the high affinity state
Method: SOLUTION NMR

PDB-6kjo:
The microtubule-binding domains of yeast cytoplasmic dynein in the low affinity state
Method: SOLUTION NMR

Source
  • sus scrofa (pig)
  • Pig (pig)
  • saccharomyces cerevisiae s288c (yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsMOTOR PROTEIN/STRUCTURAL PROTEIN / MOTOR PROTEIN-STRUCTURAL PROTEIN COMPLEX / Dynein / Microtubule / MOTOR PROTEIN / disulfide bond / high affinity / low affinity

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