3ERR

Microtubule binding domain from mouse cytoplasmic dynein as a fusion with seryl-tRNA synthetase

3ERR の概要

• エントリーDOI: 10.2210/pdb3err/pdb
• 分子名称: fusion protein of microtubule binding domain from mouse cytoplasmic dynein and seryl-tRNA synthetase from Thermus thermophilus, ADENOSINE MONOPHOSPHATE (3 entities in total)
• 機能のキーワード: dynein, microtubule binding domain, coiled coil, fusion protein, ligase
• 由来する生物種: Mus musculus; 詳細
• 細胞内の位置: Cytoplasm : P34945
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 122609.91

構造登録者

Carter, A.P. (登録日: 2008-10-03, 公開日: 2008-11-25, 最終更新日: 2023-09-06)

主引用文献

Carter, A.P.,Garbarino, J.E.,Wilson-Kubalek, E.M.,Shipley, W.E.,Cho, C.,Milligan, R.A.,Vale, R.D.,Gibbons, I.R.
Structure and functional role of dynein's microtubule-binding domain.
Science, 322:1691-1695, 2008

PubMed Abstract: Dynein motors move various cargos along microtubules within the cytoplasm and power the beating of cilia and flagella. An unusual feature of dynein is that its microtubule-binding domain (MTBD) is separated from its ring-shaped AAA+ adenosine triphosphatase (ATPase) domain by a 15-nanometer coiled-coil stalk. We report the crystal structure of the mouse cytoplasmic dynein MTBD and a portion of the coiled coil, which supports a mechanism by which the ATPase domain and MTBD may communicate through a shift in the heptad registry of the coiled coil. Surprisingly, functional data suggest that the MTBD, and not the ATPase domain, is the main determinant of the direction of dynein motility.

PubMed: 19074350
DOI: 10.1126/science.1164424

実験手法

X-RAY DIFFRACTION (2.27 Å)