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https://doi.org/10.1186/1472-6807-10-19
Title: | A kinesin motor in a force-producing conformation | Authors: | Heuston, E Bronner, C.E Kull, F.J Endow, S.A |
Keywords: | adenosine diphosphate adenosine triphosphate kinesin Drosophila protein ncd protein, Drosophila article beta sheet binding site conformational transition crystal structure kinetics microtubule point mutation protein binding protein hydrolysis protein secretion protein structure amino acid sequence amino acid substitution animal chemical structure chemistry Drosophila melanogaster genetics hydrolysis metabolism mutation protein secondary structure rotation X ray crystallography Rumex Adenosine Diphosphate Adenosine Triphosphate Amino Acid Sequence Amino Acid Substitution Animals Binding Sites Crystallography, X-Ray Drosophila melanogaster Drosophila Proteins Hydrolysis Kinesin Kinetics Microtubules Models, Molecular Mutation Protein Structure, Secondary Rotation |
Issue Date: | 2010 | Citation: | Heuston, E, Bronner, C.E, Kull, F.J, Endow, S.A (2010). A kinesin motor in a force-producing conformation. BMC Structural Biology 10 : 19. ScholarBank@NUS Repository. https://doi.org/10.1186/1472-6807-10-19 | Rights: | Attribution 4.0 International | Abstract: | Background. Kinesin motors hydrolyze ATP to produce force and move along microtubules, converting chemical energy into work by a mechanism that is only poorly understood. Key transitions and intermediate states in the process are still structurally uncharacterized, and remain outstanding questions in the field. Perturbing the motor by introducing point mutations could stabilize transitional or unstable states, providing critical information about these rarer states. Results. Here we show that mutation of a single residue in the kinesin-14 Ncd causes the motor to release ADP and hydrolyze ATP faster than wild type, but move more slowly along microtubules in gliding assays, uncoupling nucleotide hydrolysis from force generation. A crystal structure of the motor shows a large rotation of the stalk, a conformation representing a force-producing stroke of Ncd. Three C-terminal residues of Ncd, visible for the first time, interact with the central -sheet and dock onto the motor core, forming a structure resembling the kinesin-1 neck linker, which has been proposed to be the primary force-generating mechanical element of kinesin-1. Conclusions. Force generation by minus-end Ncd involves docking of the C-terminus, which forms a structure resembling the kinesin-1 neck linker. The mechanism by which the plus- and minus-end motors produce force to move to opposite ends of the microtubule appears to involve the same conformational changes, but distinct structural linkers. Unstable ADP binding may destabilize the motor-ADP state, triggering Ncd stalk rotation and C-terminus docking, producing a working stroke of the motor. © 2010 Heuston et al; licensee BioMed Central Ltd. | Source Title: | BMC Structural Biology | URI: | https://scholarbank.nus.edu.sg/handle/10635/181662 | ISSN: | 14726807 | DOI: | 10.1186/1472-6807-10-19 | Rights: | Attribution 4.0 International |
Appears in Collections: | Elements Staff Publications |
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