NDLI: Real-time Structural Transitions Are Coupled to Chemical Steps in ATP Hydrolysis by Eg5 Kinesin*

Content Provider	PubMed Central
Author	Jun, Bokkyoo Kim, Sunyoung
Abstract	At the biochemical level, motor proteins are enzymatic molecules that function by converting chemical energy into mechanical motion. The key element for energy transduction and a major unresolved question common for all motor proteins is the coordination between the chemical and conformational steps in ATP hydrolysis. Here we show time-lapse monitoring of an in vitro ATP hydrolysis reaction by the motor domain of a human Kinesin-5 protein (Eg5) using difference Fourier transform infrared spectroscopy and UV photolysis of caged ATP. In this first continuous observation of a biological reaction coordinate from substrate to product, direct spectral markers for two catalytic events are measured: proton abstraction from nucleophilic water by the catalytic base and formation of the inorganic phosphate leaving group. Simultaneous examination of conformational switching in Eg5, in parallel with catalytic steps, shows structural transitions in solution consistent with published crystal structures of the prehydrolytic and ADP-bound states. In addition, we detect structural modifications in the Eg5 motor domain during bond cleavage between the β- and γ-phosphates of ATP. This conclusion challenges mechanochemical models for motor proteins that utilize only two stages of the catalytic cycle to drive force and motion.
Related Links	http://dx.doi.org/10.1074/jbc.c110.103762
Ending Page	11077
Page Count	5
Starting Page	11073
File Format	PDF
ISSN	00219258
e-ISSN	1083351X
Journal	The Journal of Biological Chemistry
Issue Number	15
Volume Number	285
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2010-04-09
Access Restriction	Open
Rights Holder	American Society for Biochemistry and Molecular Biology
Subject Keyword	Cell Biology Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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Real-time Structural Transitions Are Coupled to Chemical Steps in ATP Hydrolysis by Eg5 Kinesin

ATP Hydrolysis in Eg5 Kinesin Involves a Catalytic Two-water Mechanism* ♦

Pathway of ATP Hydrolysis by Monomeric Kinesin Eg5†

A Two-water System♦ ATP Hydrolysis in Eg5 Kinesin Involves a Catalytic Two-water Mechanism

Dimeric Eg5 maintains processivity through alternating-site catalysis with rate-limiting ATP hydrolysis.

Eg5 steps it up!

ATP Hydrolysis in Eg5 Kinesin Involves a Catalytic Two-water Mechanism

Extensive conformational transitions are required to turn on ATP hydrolysis in myosin

Dimeric Eg5 Maintains Processivity through Alternating-site Catalysis with Rate-limiting ATP Hydrolysis* [unk]

Real-time Structural Transitions Are Coupled to Chemical Steps in ATP Hydrolysis by Eg5 Kinesin*

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Real-time Structural Transitions Are Coupled to Chemical Steps in ATP Hydrolysis by Eg5 Kinesin

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Dimeric Eg5 maintains processivity through alternating-site catalysis with rate-limiting ATP hydrolysis.

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Real-time Structural Transitions Are Coupled to Chemical Steps in ATP Hydrolysis by Eg5 Kinesin*