Structure of the Microtubule-Binding Domain of Flagellar Dynein

被引：13

作者：

Kato, Yusuke S. ^{[1
,2
,3
]}

Yagi, Toshiki ^{[4
,5
,6
]}

Harris, Sarah A. ^{[7
]}

Ohki, Shin-ya ^{[8
]}

Yura, Kei ^{[9
,10
]}

Shimizu, Youske ^{[2
]}

Honda, Shinya ^{[3
]}

Kamiya, Ritsu ^{[4
,11
]}

Burgess, Stan A. ^{[1
]}

Tanokura, Masaru ^{[2
]}

机构：

[1] Univ Leeds, Inst Mol & Cellular Biol, Inst Mol & Cellular Biol, Leeds LS2 9JT, W Yorkshire, England

[2] Univ Tokyo, Dept Appl Biol Chem, Bunkyo Ku, Tokyo 1138657, Japan

[3] Natl Inst Adv Ind Sci & Technol, Biomed Res Inst, Tsukuba, Ibaraki 3058566, Japan

[4] Univ Tokyo, Dept Biol Sci, Bunkyo Ku, Tokyo 1130033, Japan

[5] Kyoto Univ, Grad Sch Sci, Kyoto 6068502, Japan

[6] Univ Tokyo, Dept Cell Biol & Anat, Bunkyo Ku, Tokyo 1130033, Japan

[7] Univ Leeds, Sch Phys & Astron, Leeds LS2 9JT, W Yorkshire, England

[8] Japan Adv Inst Sci & Technol, CNMT, Nomi 9231292, Japan

[9] Ochanomizu Univ, Grad Sch Humanities & Sci, Bunkyo Ku, Tokyo 1128610, Japan

[10] Natl Inst Genet, Mishima, Shizuoka 4118540, Japan

[11] Japan Sci & Technol Agcy, CREST, Kawaguchi, Saitama 3320012, Japan

来源：

STRUCTURE | 2014年 / 22卷 / 11期

基金：

英国生物技术与生命科学研究理事会;

关键词：

INNER-ARM DYNEIN; COILED-COIL; MOTOR PROTEINS; IN-VITRO; KINESIN; STALK; TRANSLOCATION; ASSIGNMENT; INTERFACE; EFFICIENT;

D O I：

10.1016/j.str.2014.08.021

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 beta 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.

引用

页码：1628 / 1638

页数：11

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