The overall conformation of conventional kinesins studied by small angle X-ray and neutron scattering.
The quaternary structures of several monomeric and dimeric kinesin constructs from Homo sapiens and Drosophila melanogaster were analyzed using small angle x-ray and neutron scattering. The experimental scattering curves of these proteins were compared with simulated scattering curves calculated from available crystallographic coordinates. These comparisons indicate that the overall conformations of the solution structures of D. melanogaster and H. sapiens kinesin heavy chain dimers are compatible with the crystal structure of dimeric kinesin from Rattus norvegicus. This suggests that the unusual asymmetric conformation of dimeric kinesin in the microtubule-independent ADP state is likely to be a general feature of the kinesin heavy chain subfamily. An intermediate length Drosophila construct (365 residues) is mostly monomeric at low protein concentration whereas at higher concentrations it is dimeric with a tendency to form higher oligomers.
Kozielski
F
F
Laboratoire de Microscopie Electronique Structurale, Institut de Biologie Structurale (CEA 47 CNRS), 41, rue Jules Horowitz, 38027 Grenoble Cedex 01, France. kozielsk@lmes.ibs.fr
Svergun
D
D
Zaccai
G
G
Wade
R H
RH
Koch
M H
MH
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D019281:Dimerization; D004331:Drosophila melanogaster; D006801:Humans; D016547:Kinesins / Q000737:chemistry*; D007700:Kinetics; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009502:Neutrons; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry; D012542:Scattering, Radiation; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D017356:Synchrotrons; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D011994:Recombinant Proteins; D016547:Kinesins