3DCB

Crystal structure of the Drosophila kinesin family member NOD in complex with AMPPNP

3DCB の概要

• エントリーDOI: 10.2210/pdb3dcb/pdb
• 関連するPDBエントリー: 3DC4
• 分子名称: Kinesin-like protein Nod, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• 機能のキーワード: kinesin, catalytic domain, atpase, microtubule, amppnp, nucleotide-binding protein, atp-binding, coiled coil, motor protein, nucleotide-binding
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• 細胞内の位置: Cytoplasm, cytoskeleton (Probable): P18105
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38836.06

構造登録者

Cochran, J.C.,Mulko, N.K.,Kull, F.J. (登録日: 2008-06-03, 公開日: 2009-02-10, 最終更新日: 2023-08-30)

主引用文献

Cochran, J.C.,Sindelar, C.V.,Mulko, N.K.,Collins, K.A.,Kong, S.E.,Hawley, R.S.,Kull, F.J.
ATPase cycle of the nonmotile kinesin NOD allows microtubule end tracking and drives chromosome movement.
Cell(Cambridge,Mass.), 136:110-122, 2009

PubMed Abstract: Segregation of nonexchange chromosomes during Drosophila melanogaster meiosis requires the proper function of NOD, a nonmotile kinesin-10. We have determined the X-ray crystal structure of the NOD catalytic domain in the ADP- and AMPPNP-bound states. These structures reveal an alternate conformation of the microtubule binding region as well as a nucleotide-sensitive relay of hydrogen bonds at the active site. Additionally, a cryo-electron microscopy reconstruction of the nucleotide-free microtubule-NOD complex shows an atypical binding orientation. Thermodynamic studies show that NOD binds tightly to microtubules in the nucleotide-free state, yet other nucleotide states, including AMPPNP, are weakened. Our pre-steady-state kinetic analysis demonstrates that NOD interaction with microtubules occurs slowly with weak activation of ADP product release. Upon rapid substrate binding, NOD detaches from the microtubule prior to the rate-limiting step of ATP hydrolysis, which is also atypical for a kinesin. We propose a model for NOD's microtubule plus-end tracking that drives chromosome movement.

PubMed: 19135893
DOI: 10.1016/j.cell.2008.11.048

実験手法

X-RAY DIFFRACTION (2.5 Å)