6qus | pdb_00006qus

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

spinqualitylabelsall models 6qus, resolution 3.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6qus is a 5 chain structure with sequence from Human and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GDP, GTP, MG, TA1 Gene: CAMSAP1 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TBA1B_HUMAN] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. [TBB5_HUMAN] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. [CAMP1_HUMAN] Probable microtubule-binding protein that plays a role in the regulation of cell morphology and cytoskeletal organization. Through interaction with spectrin may regulate neurite outgrowth. Publication Abstract from PubMed 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. Structural determinants of microtubule minus end preference in CAMSAP CKK domains.,Atherton J, Luo Y, Xiang S, Yang C, Rai A, Jiang K, Stangier M, Vemu A, Cook AD, Wang S, Roll-Mecak A, Steinmetz MO, Akhmanova A, Baldus M, Moores CA Nat Commun. 2019 Nov 20;10(1):5236. doi: 10.1038/s41467-019-13247-6. PMID:31748546 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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