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 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.
| Original language | English |
|---|---|
| Pages (from-to) | 1628-1638 |
| Number of pages | 11 |
| Journal | Structure |
| Volume | 22 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - 2014 Nov 4 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Structural Biology
- Molecular Biology
Cite this
Structure of the Microtubule-Binding Domain of Flagellar Dynein. / Kato, Yusuke S.; Yagi, Toshiki; Harris, Sarah A.; Ohki, Shin Ya; Yura, Kei; Shimizu, Youské; Honda, Shinya; Kamiya, Ritsu; Burgess, Stan A.; Tanokura, Masaru.
In: Structure, Vol. 22, No. 11, 04.11.2014, p. 1628-1638.Research output: Contribution to journal › Article
}
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
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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UR - http://www.scopus.com/inward/citedby.url?scp=84908548832&partnerID=8YFLogxK
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 -