title: [Crystallography of ATP hydrolysis mechanism in rat brain kinesin].
abstract: Rat brain kinesin is a conventional kinesin that uses the energy from ATP hydrolysis to walk along the microtubule progressively. Studying how the chemical energy in ATP is utilized for mechanical movement is important to understand this moving function. The monomeric motor domain, rK354, was crystallized. An ATP analog, AMPPNP, was soaked in the active site. Comparing the complex structure of rK354 x AMPPNP and that of rK354ADP, a hypothesis is proposed that Glu237 in the Switch II region sensors the presence of gamma-phosphate and transfers the signal to the microtubule binding region.
authors.forename: Qun
authors.initials: Q
authors.lastname: Wan
authors.forename: Pingting
authors.initials: P
authors.lastname: Zhu
authors.forename: Houning
authors.initials: H
authors.lastname: Lü
authors.forename: Xinhong
authors.initials: X
authors.lastname: Chen
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism*; D000266:Adenylyl Imidodiphosphate / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000378:metabolism*; D020134:Catalytic Domain; D003461:Crystallography; D006868:Hydrolysis; D016547:Kinesins / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism; D010710:Phosphates; D011485:Protein Binding; D051381:Rats
chemical_list: D010710:Phosphates; D000266:Adenylyl Imidodiphosphate; D000255:Adenosine Triphosphate; D016547:Kinesins