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TitleNucleotide-induced global conformational changes of flagellar dynein arms revealed by in situ analysis.
Journal, issue, pagesNat Struct Mol Biol, Vol. 17, Issue 6, Page 761-767, Year 2010
Publish dateMay 9, 2010
AuthorsTandis Movassagh / Khanh Huy Bui / Hitoshi Sakakibara / Kazuhiro Oiwa / Takashi Ishikawa /
PubMed AbstractOuter and inner dynein arms generate force for the flagellar/ciliary bending motion. Although nucleotide-induced structural change of dynein heavy chains (the ATP-driven motor) was proven in vitro, ...Outer and inner dynein arms generate force for the flagellar/ciliary bending motion. Although nucleotide-induced structural change of dynein heavy chains (the ATP-driven motor) was proven in vitro, our lack of knowledge in situ has precluded an understanding of the bending mechanism. Here we reveal nucleotide-induced global structural changes of the outer and inner dynein arms of Chlamydomonas reinhardtii flagella in situ using electron cryotomography. The ATPase domains of the dynein heavy chains move toward the distal end, and the N-terminal tail bends sharply during product release. This motion could drive the adjacent microtubule to cause a sliding motion. In contrast to in vitro results, in the presence of nucleotides, outer dynein arms coexist as clusters of apo or nucleotide-bound forms in situ. This implies a cooperative switching, which may be related to the mechanism of bending.
External linksNat Struct Mol Biol / PubMed:20453857
MethodsEM (subtomogram averaging)
Resolution37.0 - 39.0 Å
Structure data

EMDB-1696:
Outer Dynein arms with a Microtubule Doublet in the absence of nucleotides
Method: EM (subtomogram averaging) / Resolution: 37.0 Å

EMDB-1697:
Outer dynein arms with a microtubule doublet in the presence of ADP.Vanadate
Method: EM (subtomogram averaging) / Resolution: 39.0 Å

Source
  • Chlamydomonas reinhardtii (plant)

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