TY - JOUR
T1 - Structure of the Microtubule-Binding Domain of Flagellar Dynein
AU - Kato, Yusuke S.
AU - Yagi, Toshiki
AU - Harris, Sarah A.
AU - Ohki, Shin Ya
AU - Yura, Kei
AU - Shimizu, Youské
AU - Honda, Shinya
AU - Kamiya, Ritsu
AU - Burgess, Stan A.
AU - Tanokura, Masaru
N1 - Funding Information:
We thank Drs. Peter J. Knight, Thomas A. Edwards, Anthony J. Roberts (University of Leeds), Keiko Hirose, and Taro Q. P. Uyeda (National Institute of Advanced Industrial Science and Technology [AIST] Japan) for their intense discussions and/or critical readings of the manuscript, Ian R. Gibbons and Joan E. Garbarino (University of California, Berkeley) for kindly providing the SRS-chimera expression systems, Masahide Kikkawa (University of Tokyo) and Ronald D. Vale (University of California, San Francisco) for kindly providing the 3D EM map and suggestions, Ken Downing (Lawrence Berkeley Laboratory) for kindly providing microtubule coordinates, and Jun-ichi Kurita (Agilent Technologies Japan, Ltd.), Takashi Shimizu, and Kenji Kanazawa (AIST Japan) for their dedicated technical support. Maintenance of the 750 MHz-NMR spectrometer used in this work has been supported by the Center for Nano Materials and Technology and the Japan Advanced Institute of Science and Technology. Y.S.K. was supported in part by the Biotechnology and Biological Sciences Research Council, United Kingdom (to S.A.B.). K.Y. was supported by Platform for Drug Discovery, Informatics, and Structural Life Science from the Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan. This work was supported in part by the National Project on Protein Structural and Functional Analysis, Targeted Proteins Research Program, and Grant-in-Aid for Scientific Research, of MEXT of Japan.
PY - 2014/11/4
Y1 - 2014/11/4
N2 - Flagellar dyneins are essential microtubule motors in eukaryotes, as they drive the beating motions of cilia and flagella. Unlike myosin and kinesin motors, the track binding mechanism of dyneins and the regulation between the strong and weak binding states remain obscure. Here we report the solution structure of the microtubule-binding domain of flagellar dynein-c/DHC9 (dynein-c MTBD). The structure reveals a similar overall helix-rich fold to that of the MTBD of cytoplasmic dynein (cytoplasmic MTBD), but dynein-c MTBD has an additional flap, consisting of an antiparallel β sheet. The flap is positively charged and highly flexible. Despite the structural similarity to cytoplasmic MTBD, dynein-c MTBD shows only a small change in the microtubule-binding affinity depending on the registry change of coiled coil-sliding, whereby lacks the apparent strong binding state. The surface charge distribution of dynein-c MTBD also differs from that of cytoplasmic MTBD, which suggests a difference in the microtubule-binding mechanism.
AB - Flagellar dyneins are essential microtubule motors in eukaryotes, as they drive the beating motions of cilia and flagella. Unlike myosin and kinesin motors, the track binding mechanism of dyneins and the regulation between the strong and weak binding states remain obscure. Here we report the solution structure of the microtubule-binding domain of flagellar dynein-c/DHC9 (dynein-c MTBD). The structure reveals a similar overall helix-rich fold to that of the MTBD of cytoplasmic dynein (cytoplasmic MTBD), but dynein-c MTBD has an additional flap, consisting of an antiparallel β sheet. The flap is positively charged and highly flexible. Despite the structural similarity to cytoplasmic MTBD, dynein-c MTBD shows only a small change in the microtubule-binding affinity depending on the registry change of coiled coil-sliding, whereby lacks the apparent strong binding state. The surface charge distribution of dynein-c MTBD also differs from that of cytoplasmic MTBD, which suggests a difference in the microtubule-binding mechanism.
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U2 - 10.1016/j.str.2014.08.021
DO - 10.1016/j.str.2014.08.021
M3 - Article
C2 - 25450768
AN - SCOPUS:84908548832
VL - 22
SP - 1628
EP - 1638
JO - Structure with Folding & design
JF - Structure with Folding & design
SN - 0969-2126
IS - 11
ER -