6QUY
NgCKK (N.Gruberi CKK) decorated 13pf taxol-GDP microtubule
Summary for 6QUY
Entry DOI | 10.2210/pdb6quy/pdb |
Related | 6QUS |
EMDB information | 4643 4644 |
Descriptor | Tubulin alpha-1B chain, CKK domain protein, Tubulin beta chain, ... (7 entities in total) |
Functional Keywords | microtubule camsap calmodulin-regulated spectrum-associated proteins ckk cryo-em cryo-electron microscopy, structural protein |
Biological source | Naegleria gruberi (Amoeba) More |
Total number of polymer chains | 5 |
Total formula weight | 224412.38 |
Authors | Atherton, J.M.,Luo, Y.,Xiang, S.,Yang, C.,Jiang, K.,Stangier, M.,Vemu, A.,Cook, A.,Wang, S.,Roll-Mecak, A.,Steinmetz, M.O.,Akhmanova, A.,Baldus, M.,Moores, C.A. (deposition date: 2019-02-28, release date: 2019-11-27, Last modification date: 2024-05-15) |
Primary citation | 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: 31748546DOI: 10.1038/s41467-019-13247-6 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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