4F6R

Tubulin:Stathmin-like domain complex

Summary for 4F6R

• Entry DOI: 10.2210/pdb4f6r/pdb
• Related: 4F61
• Descriptor: Tubulin alpha chain, Tubulin beta chain, Stathmin-like domain R1, ... (10 entities in total)
• Functional Keywords: alpha-tubulin, beta-tubulin, gtpase, microtubule, rb3, stathmin s-tubulin, subtilisin, tubulin, cell cycle
• Biological source: Artificial gene; More
• Total number of polymer chains: 4
• Total formula weight: 129788.10

Authors

Gigant, B.,Mignot, I.,Knossow, M. (deposition date: 2012-05-15, release date: 2012-07-18, Last modification date: 2023-09-13)

Primary citation

Mignot, I.,Pecqueur, L.,Dorleans, A.,Karuppasamy, M.,Ravelli, R.B.,Dreier, B.,Pluckthun, A.,Knossow, M.,Gigant, B.
Design and characterization of modular scaffolds for tubulin assembly.
J.Biol.Chem., 287:31085-31094, 2012

PubMed Abstract: In cells, microtubule dynamics is regulated by stabilizing and destabilizing factors. Whereas proteins in both categories have been identified, their mechanism of action is rarely understood at the molecular level. This is due in part to the difficulties faced in structural approaches to obtain atomic models when tubulin is involved. Here, we design and characterize new stathmin-like domain (SLD) proteins that sequester tubulins in numbers different from two, the number of tubulins bound by stathmin or by the SLD of RB3, two stathmin family members that have been extensively studied. We established rules for the design of tight tubulin-SLD assemblies and applied them to complexes containing one to four tubulin heterodimers. Biochemical and structural experiments showed that the engineered SLDs behaved as expected. The new SLDs will be tools for structural studies of microtubule regulation. The larger complexes will be useful for cryo-electron microscopy, whereas crystallography or nuclear magnetic resonance will benefit from the 1:1 tubulin-SLD assembly. Finally, our results provide new insight into SLD function, suggesting that a major effect of these phosphorylatable proteins is the programmed release of sequestered tubulin for microtubule assembly at the specific cellular locations of members of the stathmin family.

PubMed: 22791712
DOI: 10.1074/jbc.M112.383869

Experimental method

X-RAY DIFFRACTION (2.64 Å)