2M02

3D structure of cap-gly domain of mammalian dynactin determined by magic angle spinning NMR spectroscopy

2M02 の概要

• エントリーDOI: 10.2210/pdb2m02/pdb
• NMR情報: BMRB: 17937
• 分子名称: Dynactin subunit 1 (1 entity in total)
• 機能のキーワード: motor protein
• 由来する生物種: Rattus norvegicus (brown rat,rat,rats)
• 細胞内の位置: Cytoplasm: P28023
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9525.58

構造登録者

Yan, S.,Hou, G.,Schwieters, C.D.,Ahmed, S.,Williams, J.C.,Polenova, T. (登録日: 2012-10-15, 公開日: 2013-05-08, 最終更新日: 2024-05-15)

主引用文献

Yan, S.,Hou, G.,Schwieters, C.D.,Ahmed, S.,Williams, J.C.,Polenova, T.
Three-Dimensional Structure of CAP-Gly Domain of Mammalian Dynactin Determined by Magic Angle Spinning NMR Spectroscopy: Conformational Plasticity and Interactions with End-Binding Protein EB1.
J.Mol.Biol., 425:4249-4266, 2013

PubMed Abstract: Microtubules and their associated proteins play important roles in vesicle and organelle transport, cell motility and cell division. Perturbation of these processes by mutation typically gives rise to severe pathological conditions. In our efforts to obtain atomic information on microtubule-associated protein/microtubule interactions with the goal to understand mechanisms that might potentially assist in the development of treatments for these diseases, we have determined the three-dimensional structure of CAP-Gly (cytoskeleton-associated protein, glycine-rich) domain of mammalian dynactin by magic angle spinning NMR spectroscopy. We observe two conformations in the β2 strand encompassing residues T43-V44-A45, residues that are adjacent to the disease-associated mutation, G59S. Upon binding of CAP-Gly to microtubule plus-end tracking protein EB1, the CAP-Gly shifts to a single conformer. We find extensive chemical shift perturbations in several stretches of residues of CAP-Gly upon binding to EB1, from which we define accurately the CAP-Gly/EB1 binding interface. We also observe that the loop regions may exhibit unique flexibility, especially in the GKNDG motif, which participates in the microtubule binding. This study in conjunction with our previous reports suggests that conformational plasticity is an intrinsic property of CAP-Gly likely due to its unusually high loop content and may be required for its biological functions.

PubMed: 23648839
DOI: 10.1016/j.jmb.2013.04.027

実験手法

SOLID-STATE NMR