Closing of the nucleotide pocket of kinesin-family motors upon binding to microtubules.

@article{citeulike:1512118, abstract = {We have used adenosine diphosphate analogs containing electron paramagnetic resonance (EPR) spin moieties and EPR spectroscopy to show that the nucleotide-binding site of kinesin-family motors closes when the motor.diphosphate complex binds to microtubules. Structural analyses demonstrate that a domain movement in the switch 1 region at the nucleotide site, homologous to domain movements in the switch 1 region in the G proteins [heterotrimeric guanine nucleotide-binding proteins], explains the EPR data. The switch movement primes the motor both for the free energy-yielding nucleotide hydrolysis reaction and for subsequent conformational changes that are crucial for the generation of force and directed motion along the microtubule.}, address = {Department of Biochemistry, University of California, San Francisco, CA 94143, USA. naber@itsa.ucsf.edu}, author = {Naber, N. and Minehardt, T. J. and Rice, S. and Chen, X. and Grammer, J. and Matuska, M. and Vale, R. D. and Kollman, P. A. and Car, R. and Yount, R. G. and Cooke, R. and Pate, E. }, citeulike-article-id = {1512118}, comment = {PDB file 1ozx, "MODEL OF THE MICROTUBULE MOTOR, NCD, WITH SWITCH 1 CLOSED AND WITH ADP BOUND AT THE NUCLEOTIDE SITE"}, doi = {http://dx.doi.org/10.1126/science.1082374}, issn = {1095-9203}, journal = {Science}, keywords = {kinesin, structure}, month = {May}, number = {5620}, pages = {798--801}, posted-at = {2007-07-30 02:47:14}, priority = {0}, title = {Closing of the nucleotide pocket of kinesin-family motors upon binding to microtubules.}, url = {http://dx.doi.org/10.1126/science.1082374}, volume = {300}, year = {2003} }

TY - JOUR ID - citeulike:1512118 L3 - citeulike-article-id:1512118 TI - Closing of the nucleotide pocket of kinesin-family motors upon binding to microtubules. JF - Science VL - 300 IS - 5620 SP - 798 EP - 801 AD - Department of Biochemistry, University of California, San Francisco, CA 94143, USA. naber@itsa.ucsf.edu SN - 1095-9203 N2 - We have used adenosine diphosphate analogs containing electron paramagnetic resonance (EPR) spin moieties and EPR spectroscopy to show that the nucleotide-binding site of kinesin-family motors closes when the motor.diphosphate complex binds to microtubules. Structural analyses demonstrate that a domain movement in the switch 1 region at the nucleotide site, homologous to domain movements in the switch 1 region in the G proteins [heterotrimeric guanine nucleotide-binding proteins], explains the EPR data. The switch movement primes the motor both for the free energy-yielding nucleotide hydrolysis reaction and for subsequent conformational changes that are crucial for the generation of force and directed motion along the microtubule. KW - kinesin KW - structure N1 - PDB file 1ozx, "MODEL OF THE MICROTUBULE MOTOR, NCD, WITH SWITCH 1 CLOSED AND WITH ADP BOUND AT THE NUCLEOTIDE SITE" AU - Naber, N AU - Minehardt, TJ AU - Rice, S AU - Chen, X AU - Grammer, J AU - Matuska, M AU - Vale, RD AU - Kollman, PA AU - Car, R AU - Yount, RG AU - Cooke, R AU - Pate, E PY - 2003/05/02/ UR - http://dx.doi.org/10.1126/science.1082374 ER -