6GWC

Tubulin:iE5 alphaRep complex

Summary for 6GWC

• Entry DOI: 10.2210/pdb6gwc/pdb
• Descriptor: ALPHA-TUBULIN, Tubulin beta chain, iE5 ALPHAREP, ... (8 entities in total)
• Functional Keywords: microtubule, artificial protein, alpharep, cytoskeleton, cell cycle
• Biological source: synthetic construct; More
• Total number of polymer chains: 3
• Total formula weight: 127013.68

Authors

Gigant, B.,Campanacci, V. (deposition date: 2018-06-22, release date: 2019-01-30, Last modification date: 2024-01-17)

Primary citation

Campanacci, V.,Urvoas, A.,Consolati, T.,Cantos-Fernandes, S.,Aumont-Nicaise, M.,Valerio-Lepiniec, M.,Surrey, T.,Minard, P.,Gigant, B.
Selection and Characterization of Artificial Proteins Targeting the Tubulin alpha Subunit.
Structure, 27:497-506.e4, 2019

PubMed Abstract: Microtubules are cytoskeletal filaments of eukaryotic cells made of αβ-tubulin heterodimers. Structural studies of non-microtubular tubulin rely mainly on molecules that prevent its self-assembly and are used as crystallization chaperones. Here we identified artificial proteins from an αRep library that are specific to α-tubulin. Turbidity experiments indicate that these αReps impede microtubule assembly in a dose-dependent manner and total internal reflection fluorescence microscopy further shows that they specifically block growth at the microtubule (-) end. Structural data indicate that they do so by targeting the α-tubulin longitudinal surface. Interestingly, in one of the complexes studied, the α subunit is in a conformation that is intermediate between the ones most commonly observed in X-ray structures of tubulin and those seen in the microtubule, emphasizing the plasticity of tubulin. These α-tubulin-specific αReps broaden the range of tools available for the mechanistic study of microtubule dynamics and its regulation.

PubMed: 30661854
DOI: 10.1016/j.str.2018.12.001

Experimental method

X-RAY DIFFRACTION (2.6 Å)