5LZN

-TIP microtubule-binding domain

Summary for 5LZN

• Entry DOI: 10.2210/pdb5lzn/pdb
• Descriptor: Calmodulin-regulated spectrin-associated protein 3 (2 entities in total)
• Functional Keywords: -tip, microtubule, structural protein
• Biological source: Mus musculus (House Mouse)
• Total number of polymer chains: 1
• Total formula weight: 13560.57

Authors

Stangier, M.M.,Steinmetz, M.O. (deposition date: 2016-09-30, release date: 2017-10-04, Last modification date: 2024-01-17)

Primary citation

Atherton, J.,Jiang, K.,Stangier, M.M.,Luo, Y.,Hua, S.,Houben, K.,van Hooff, J.J.E.,Joseph, A.P.,Scarabelli, G.,Grant, B.J.,Roberts, A.J.,Topf, M.,Steinmetz, M.O.,Baldus, M.,Moores, C.A.,Akhmanova, A.
A structural model for microtubule minus-end recognition and protection by CAMSAP proteins.
Nat. Struct. Mol. Biol., 24:931-943, 2017

PubMed Abstract: CAMSAP and Patronin family members regulate microtubule minus-end stability and localization and thus organize noncentrosomal microtubule networks, which are essential for cell division, polarization and differentiation. Here, we found that the CAMSAP C-terminal CKK domain is widely present among eukaryotes and autonomously recognizes microtubule minus ends. Through a combination of structural approaches, we uncovered how mammalian CKK binds between two tubulin dimers at the interprotofilament interface on the outer microtubule surface. In vitro reconstitution assays combined with high-resolution fluorescence microscopy and cryo-electron tomography suggested that CKK preferentially associates with the transition zone between curved protofilaments and the regular microtubule lattice. We propose that minus-end-specific features of the interprotofilament interface at this site serve as the basis for CKK's minus-end preference. The steric clash between microtubule-bound CKK and kinesin motors explains how CKK protects microtubule minus ends against kinesin-13-induced depolymerization and thus controls the stability of free microtubule minus ends.

PubMed: 28991265
DOI: 10.1038/nsmb.3483

Experimental method

X-RAY DIFFRACTION (1.4 Å)