Configuration of the two kinesin motor domains during ATP hydrolysis

Research output: Contribution to journalArticle

65 Citations (Scopus)

Abstract

To understand the mechanism of kinesin movement we have investigated the relative configuration of the two kinesin motor domains during ATP hydrolysis using fluorescence polarization microscopy of ensemble and single molecules. We found that: (i) in nucleotide states that induce strong microtubule binding, both motor domains are bound to the microtubule with similar orientations; (ii) this orientation is maintained during processive motion in the presence of ATP; (iii) the neck-linker region of the motor domain has distinct configurations for each nucleotide condition tested. Our results fit well with a hand-over-hand type movement mechanism and suggest how the ATPase cycle in the two motor domains is coordinated. We propose that the motor neck-linker domain configuration controls ADP release.

Original languageEnglish (US)
Pages (from-to)836-842
Number of pages7
JournalNature Structural Biology
Volume10
Issue number10
DOIs
StatePublished - Oct 1 2003

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Kinesin
Microtubules
Hydrolysis
Neck
Nucleotides
Hand
Adenosine Triphosphate
Polarization Microscopy
Fluorescence Polarization
Fluorescence Microscopy
Adenosine Diphosphate
Adenosine Triphosphatases
Microscopic examination
Fluorescence
Polarization
Molecules

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Genetics

Cite this

Configuration of the two kinesin motor domains during ATP hydrolysis. / Asenjo, Ana B.; Krohn, Natan; Sosa, Hernando J.

In: Nature Structural Biology, Vol. 10, No. 10, 01.10.2003, p. 836-842.

Research output: Contribution to journalArticle

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