title: 3D electron microscopy of the interaction of kinesin with tubulin.
abstract: We have studied the structure of microtubules decorated with kinesin motor domains in different nucleotide states by 3D electron microscopy. Having docked the atomic coordinates of both dimeric ADP.kinesin and tubulin heterodimer into a map of kinesin dimers bound to microtubules in the presence of ADP, we try to predict which regions of the proteins interact in the weakly binding state. When either the presence of 5'-adenylyimidodiphosphate (AMP-PNP) or an absence of nucleotides puts motor domains into a strongly-bound state, the 3D maps show changes in the motor domains which modify their interaction with beta-tubulin. The maps also show differences in beta-tubulin conformation compared with undecorated microtubules or those decorated with weakly-bound motors. Strongly-bound ncd appears to produce an identical change.
authors.affiliation: Natl Inst Advanced Interdisciplinary Res, Tsukuba, Ibaraki, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Hirose
authors.forename: J
authors.initials: J
authors.lastname: Löwe
authors.forename: M
authors.initials: M
authors.lastname: Alonso
authors.forename: R A
authors.initials: RA
authors.lastname: Cross
authors.forename: L A
authors.initials: LA
authors.lastname: Amos
mesh_terms: D000244:Adenosine Diphosphate / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D001081:Apyrase / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites / Q000502:physiology; D020285:Cryoelectron Microscopy; D005583:Fourier Analysis; D006593:Hexokinase / Q000737:chemistry / Q000378:metabolism; D007091:Image Processing, Computer-Assisted; D021621:Imaging, Three-Dimensional; D016547:Kinesins / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D008854:Microscopy, Electron / Q000379:methods*; D008855:Microscopy, Electron, Scanning; D008868:Microtubule Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D008870:Microtubules / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D017239:Paclitaxel / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013552:Swine; D014404:Tubulin / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure
chemical_list: D008868:Microtubule Proteins; D020409:Molecular Motor Proteins; D014404:Tubulin; D000244:Adenosine Diphosphate; D006593:Hexokinase; D001081:Apyrase; D016547:Kinesins; D017239:Paclitaxel