7Q1F

CPAP:TUBULIN:IE5 ALPHAREP COMPLEX

Summary for 7Q1F

• Entry DOI: 10.2210/pdb7q1f/pdb
• Related: 7Q1E 7Z0F 7Z0G
• Descriptor: Tubulin alpha chain, CITRATE ANION, Tubulin beta chain, ... (11 entities in total)
• Functional Keywords: microtubule, centromere protein j, centriole, cell cycle
• Biological source: synthetic construct; More
• Total number of polymer chains: 10
• Total formula weight: 321460.79

Authors

Campanacci, V.,Gigant, b. (deposition date: 2021-10-19, release date: 2022-04-20, Last modification date: 2024-01-31)

Primary citation

Campanacci, V.,Urvoas, A.,Ammar Khodja, L.,Aumont-Nicaise, M.,Noiray, M.,Lachkar, S.,Curmi, P.A.,Minard, P.,Gigant, B.
Structural convergence for tubulin binding of CPAP and vinca domain microtubule inhibitors.
Proc.Natl.Acad.Sci.USA, 119:e2120098119-e2120098119, 2022

PubMed Abstract: Microtubule dynamics is regulated by various cellular proteins and perturbed by small-molecule compounds. To what extent the mechanism of the former resembles that of the latter is an open question. We report here structures of tubulin bound to the PN2-3 domain of CPAP, a protein controlling the length of the centrioles. We show that an α-helix of the PN2-3 N-terminal region binds and caps the longitudinal surface of the tubulin β subunit. Moreover, a PN2-3 N-terminal stretch lies in a β-tubulin site also targeted by fungal and bacterial peptide-like inhibitors of the vinca domain, sharing a very similar binding mode with these compounds. Therefore, our results identify several characteristic features of cellular partners that bind to this site and highlight a structural convergence of CPAP with small-molecule inhibitors of microtubule assembly.

PubMed: 35507869
DOI: 10.1073/pnas.2120098119

Experimental method

X-RAY DIFFRACTION (2.347 Å)