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6QVE

NgCKK (Naegleria Gruberi CKK) decorated 14pf taxol-GDP microtubule

6QVE の概要
エントリーDOI10.2210/pdb6qve/pdb
関連するPDBエントリー6QUS 6QUY
EMDBエントリー4643 4644 4650
分子名称Tubulin alpha-1B chain, Predicted protein, Beta1-tubulin, ... (7 entities in total)
機能のキーワードmicrotubule camsap calmodulin-regulated spectrum-associated proteins ckk cryo-em cryo-electron microscopy, structural protein
由来する生物種Naegleria gruberi (Amoeba)
詳細
タンパク質・核酸の鎖数5
化学式量合計224412.38
構造登録者
主引用文献Atherton, J.,Luo, Y.,Xiang, S.,Yang, C.,Rai, A.,Jiang, K.,Stangier, M.,Vemu, A.,Cook, A.D.,Wang, S.,Roll-Mecak, A.,Steinmetz, M.O.,Akhmanova, A.,Baldus, M.,Moores, C.A.
Structural determinants of microtubule minus end preference in CAMSAP CKK domains.
Nat Commun, 10:5236-5236, 2019
Cited by
PubMed Abstract: CAMSAP/Patronins regulate microtubule minus-end dynamics. Their end specificity is mediated by their CKK domains, which we proposed recognise specific tubulin conformations found at minus ends. To critically test this idea, we compared the human CAMSAP1 CKK domain (HsCKK) with a CKK domain from Naegleria gruberi (NgCKK), which lacks minus-end specificity. Here we report near-atomic cryo-electron microscopy structures of HsCKK- and NgCKK-microtubule complexes, which show that these CKK domains share the same protein fold, bind at the intradimer interprotofilament tubulin junction, but exhibit different footprints on microtubules. NMR experiments show that both HsCKK and NgCKK are remarkably rigid. However, whereas NgCKK binding does not alter the microtubule architecture, HsCKK remodels its microtubule interaction site and changes the underlying polymer structure because the tubulin lattice conformation is not optimal for its binding. Thus, in contrast to many MAPs, the HsCKK domain can differentiate subtly specific tubulin conformations to enable microtubule minus-end recognition.
PubMed: 31748546
DOI: 10.1038/s41467-019-13247-6
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.7 Å)
構造検証レポート
Validation report summary of 6qve
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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