Closing of the nucleotide pocket of kinesin-family motors upon binding to microtubules |
| |
Authors: | Naber Nariman Minehardt Todd J Rice Sarah Chen Xiaoru Grammer Jean Matuska Marija Vale Ronald D Kollman Peter A Car Roberto Yount Ralph G Cooke Roger Pate Edward |
| |
Institution: | Department of Biochemistry, University of California, San Francisco, CA 94143, USA. naber@itsa.ucsf.edu |
| |
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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|