3RYH

GMPCPP-Tubulin: RB3 Stathmin-like domain complex

Summary for 3RYH

• Entry DOI: 10.2210/pdb3ryh/pdb
• Related: 3RYC 3RYF 3RYI
• Descriptor: Tubulin alpha chain, Tubulin beta chain, Stathmin-4, ... (8 entities in total)
• Functional Keywords: alpha-tubulin, beta-tubulin, gmpcpp, gtpase, microtubule, stathmin s-tubulin, subtilisin, tubulin, cell cycle
• Biological source: Rattus norvegicus (rat); More
• Total number of polymer chains: 5
• Total formula weight: 220197.11

Authors

Nawrotek, A.,Knossow, M.,Gigant, B. (deposition date: 2011-05-11, release date: 2011-10-05, Last modification date: 2024-11-20)

Primary citation

Nawrotek, A.,Knossow, M.,Gigant, B.
The Determinants That Govern Microtubule Assembly from the Atomic Structure of GTP-Tubulin.
J.Mol.Biol., 412:35-42, 2011

PubMed Abstract: Tubulin alternates between a soluble curved structure and a microtubule straight conformation. GTP binding to αβ-tubulin is required for microtubule assembly, but whether this triggers conversion into a straighter structure is still debated. This is due, at least in part, to the lack of structural data for GTP-tubulin before assembly. Here, we report atomic-resolution crystal structures of soluble tubulin in the GDP and GTP nucleotide states in a complex with a stathmin-like domain. The structures differ locally in the neighborhood of the nucleotide. A loop movement in GTP-bound tubulin favors its recruitment to the ends of growing microtubules and facilitates its curved-to-straight transition, but this conversion has not proceeded yet. The data therefore argue for the conformational change toward the straight structure occurring as microtubule-specific contacts are established. They also suggest a model for the way the tubulin structure is modified in relation to microtubule assembly.

PubMed: 21787788
DOI: 10.1016/j.jmb.2011.07.029

Experimental method

X-RAY DIFFRACTION (2.8 Å)