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  Microtubule assembly governed by tubulin allosteric gain in flexibility and lattice induced fit.

Igaev, M., & Grubmüller, H. (2018). Microtubule assembly governed by tubulin allosteric gain in flexibility and lattice induced fit. eLife, 7: e34353. doi:10.7554/eLife.34353.

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Igaev, M.1, Autor           
Grubmüller, H.1, Autor           
Affiliations:
1Department of Theoretical and Computational Biophysics, MPI for Biophysical Chemistry, Max Planck Society, ou_578631              

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Schlagwörter: molecular biophysics; none; structural biology
 Zusammenfassung: Microtubules (MTs) are key components of the cytoskeleton and play a central role in cell division and development. MT assembly is known to be associated with a structural change in αβ-tubulin dimers from kinked to straight conformations. How GTP binding renders individual dimers polymerization-competent, however, is still unclear. Here, we have characterized the conformational dynamics and energetics of unassembled tubulin using atomistic molecular dynamics and free energy calculations. Contradictory to existing allosteric and lattice models, we find that GTP-tubulin favors a broad range of almost isoenergetic curvatures, whereas GDP-tubulin has a much lower bending flexibility. Moreover, irrespective of the bound nucleotide and curvature, two conformational states exist differing in location of the anchor point connecting the monomers that affects tubulin bending, with one state being strongly favored in solution. Our findings suggest a new combined model in which MTs incorporate and stabilize flexible GTP-dimers with a specific anchor point state.

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Sprache(n): eng - English
 Datum: 2018-04-13
 Publikationsstatus: Online veröffentlicht
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 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.7554/eLife.34353
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Titel: eLife
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: -
Seiten: 21 Band / Heft: 7 Artikelnummer: e34353 Start- / Endseite: - Identifikator: -