6FC5

Bik1 CAP-Gly domain

Summary for 6FC5

• Entry DOI: 10.2210/pdb6fc5/pdb
• Descriptor: Microtubule-associated protein (2 entities in total)
• Functional Keywords: +tip, cap-gly, microtubule, yeast, cell cycle
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 11357.17

Authors

Kumar, A.,Stangier, M.M.,Steinmetz, M.O. (deposition date: 2017-12-20, release date: 2018-04-11, Last modification date: 2024-05-08)

Primary citation

Stangier, M.M.,Kumar, A.,Chen, X.,Farcas, A.M.,Barral, Y.,Steinmetz, M.O.
Structure-Function Relationship of the Bik1-Bim1 Complex.
Structure, 26:607-618.e4, 2018

PubMed Abstract: In budding yeast, the microtubule plus-end tracking proteins Bik1 (CLIP-170) and Bim1 (EB1) form a complex that interacts with partners involved in spindle positioning, including Stu2 and Kar9. Here, we show that the CAP-Gly and coiled-coil domains of Bik1 interact with the C-terminal ETF peptide of Bim1 and the C-terminal tail region of Stu2, respectively. The crystal structures of the CAP-Gly domain of Bik1 (Bik1CG) alone and in complex with an ETF peptide revealed unique, functionally relevant CAP-Gly elements, establishing Bik1CG as a specific C-terminal phenylalanine recognition domain. Unlike the mammalian CLIP-170-EB1 complex, Bik1-Bim1 forms ternary complexes with the EB1-binding motifs SxIP and LxxPTPh, which are present in diverse proteins, including Kar9. Perturbation of the Bik1-Bim1 interaction in vivo affected Bik1 localization and astral microtubule length. Our results provide insight into the role of the Bik1-Bim1 interaction for cell division, and demonstrate that the CLIP-170-EB1 module is evolutionarily flexible.

PubMed: 29576319
DOI: 10.1016/j.str.2018.03.003

Experimental method

X-RAY DIFFRACTION (1.88 Å)