title: Structure of the microtubule-binding domain of flagellar dynein.
abstract: 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 b 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.
authors.forename: Yusuke S
authors.initials: YS
authors.lastname: Kato
authors.forename: Toshiki
authors.initials: T
authors.lastname: Yagi
authors.forename: Sarah A
authors.initials: SA
authors.lastname: Harris
authors.forename: Shin-ya
authors.initials: SY
authors.lastname: Ohki
authors.forename: Kei
authors.initials: K
authors.lastname: Yura
authors.forename: Youské
authors.initials: Y
authors.lastname: Shimizu
authors.forename: Shinya
authors.initials: S
authors.lastname: Honda
authors.forename: Ritsu
authors.initials: R
authors.lastname: Kamiya
authors.forename: Stan A
authors.initials: SA
authors.lastname: Burgess
authors.forename: Masaru
authors.initials: M
authors.lastname: Tanokura
mesh_terms: D001665:Binding Sites; D016825:Chlamydomonas reinhardtii / Q000378:metabolism*; D004398:Dyneins / Q000737:chemistry* / Q000378:metabolism; D008870:Microtubules / Q000378:metabolism*; D056004:Molecular Dynamics Simulation; D010940:Plant Proteins / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary
chemical_list: D010940:Plant Proteins; D004398:Dyneins