6QUS

HsCKK (human CAMSAP1) decorated 13pf taxol-GDP microtubule

Summary for 6QUS

• Entry DOI: 10.2210/pdb6qus/pdb
• EMDB information: 4643
• Descriptor: Tubulin alpha-1B chain, Calmodulin-regulated spectrin-associated protein 1, 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: Homo sapiens (Human); More
• Total number of polymer chains: 5
• Total formula weight: 223162.00

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

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

Experimental method

ELECTRON MICROSCOPY (3.7 Å)