ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy.
Nat Struct Biol
; 8(6): 540-4, 2001 Jun.
Article
in En
| MEDLINE
| ID: mdl-11373624
ABSTRACT
Kinesin is an ATP-driven molecular motor protein that moves processively along microtubules. Despite considerable research, the detailed mechanism of kinesin motion remains elusive. We applied an enhanced suite of single- and multiple-molecule fluorescence polarization microscopy assays to report the orientation and mobility of kinesin molecules bound to microtubules as a function of nucleotide state. In the presence of analogs of ATP, ADP-Pi or in the absence of nucleotide, the kinesin head maintains a rigid orientation. In the presence of ADP, the motor domain of kinesin, still bound to the microtubule, adopts a previously undescribed, highly mobile state. This state may be general to the chemomechanical cycle of motor proteins; in the case of kinesin, the transition from a highly mobile to a rigid state after ADP release may contribute to the generation of the 8 nm step.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Adenosine Diphosphate
/
Kinesins
/
Molecular Motor Proteins
/
Microtubules
Limits:
Humans
Language:
En
Journal:
Nat Struct Biol
Journal subject:
BIOLOGIA MOLECULAR
Year:
2001
Document type:
Article
Affiliation country:
Estados Unidos