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          Institute: MPI für molekulare Zellbiologie und Genetik     Collection: Publikationen MPI-CBG 2011-arch     Display Documents



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ID: 585240.0, MPI für molekulare Zellbiologie und Genetik / Publikationen MPI-CBG 2011-arch
Loop L5 acts as a conformational latch in the mitotic kinesin Eg5.
Authors:Behnke-Parks, William M; Vendome, Jeremie; Honig, Barry; Maliga, Zoltan; Moores, Carolyn; Rosenfeld, Steven S
Date of Publication (YYYY-MM-DD):2011
Title of Journal:The Journal of Biological Chemistry
Volume:286
Issue / Number:7
Start Page:5242
End Page:5253
Copyright:not available
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:All members of the kinesin superfamily of molecular motors contain an unusual structural motif consisting of an α-helix that is interrupted by a flexible loop, referred to as L5. We have examined the function of L5 in the mitotic kinesin Eg5 by combining site-directed mutagenesis of L5 with transient state kinetics, molecular dynamics simulations, and docking using cryo electron microscopy density. We find that mutation of a proline residue located at a turn within this loop profoundly slows nucleotide-induced structural changes both at the catalytic site as well as at the microtubule binding domain and the neck linker. Molecular dynamics simulations reveal that this mutation affects the dynamics not only of L5 itself but also of the switch I structural elements that sense ATP binding to the catalytic site. Our results lead us to propose that L5 regulates the rate of conformational change in key elements of the nucleotide binding site through its interactions with α3 and in so doing controls the speed of movement and force generation in kinesin motors.
External Publication Status:published
Document Type:Article
Version Comment:Automatic journal name synchronization
Communicated by:thuem
Affiliations:MPI für molekulare Zellbiologie und Genetik
Identifiers:LOCALID:4670
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