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-Structure paper
タイトル | Structural determinants of microtubule minus end preference in CAMSAP CKK domains. |
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ジャーナル・号・ページ | Nat Commun, Vol. 10, Issue 1, Page 5236, Year 2019 |
掲載日 | 2019年11月20日 |
著者 | Joseph Atherton / Yanzhang Luo / Shengqi Xiang / Chao Yang / Ankit Rai / Kai Jiang / Marcel Stangier / Annapurna Vemu / Alexander D Cook / Su Wang / Antonina Roll-Mecak / Michel O Steinmetz / Anna Akhmanova / Marc Baldus / Carolyn A Moores / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:31748546 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.7 - 3.8 Å |
構造データ | EMDB-4643, PDB-6qus: EMDB-4644, PDB-6quy: |
化合物 | ChemComp-GTP: ChemComp-MG: ChemComp-GDP: ChemComp-TA1: |
由来 |
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キーワード | STRUCTURAL PROTEIN / Microtubule CAMSAP Calmodulin-regulated spectrum-associated proteins CKK Cryo-EM Cryo-Electron Microscopy |