3J6E

Energy minimized average structure of Microtubules stabilized by GmpCpp

Summary for 3J6E

• Entry DOI: 10.2210/pdb3j6e/pdb
• Related: 3J6F 3J6G
• EMDB information: 5895 5896 5897 5898 5899
• Descriptor: Tubulin alpha-1A chain, Tubulin beta chain, GUANOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: microtubule, gmpcpp, structural protein
• Biological source: Sus scrofa (pig); More
• Total number of polymer chains: 18
• Total formula weight: 880235.38

Authors

Alushin, G.M.,Lander, G.C.,Kellogg, E.H.,Zhang, R.,Baker, D.,Nogales, E. (deposition date: 2014-02-18, release date: 2014-06-04, Last modification date: 2024-02-21)

Primary citation

Alushin, G.M.,Lander, G.C.,Kellogg, E.H.,Zhang, R.,Baker, D.,Nogales, E.
High-Resolution Microtubule Structures Reveal the Structural Transitions in alpha beta-Tubulin upon GTP Hydrolysis.
Cell(Cambridge,Mass.), 157:1117-1129, 2014

PubMed Abstract: Dynamic instability, the stochastic switching between growth and shrinkage, is essential for microtubule function. This behavior is driven by GTP hydrolysis in the microtubule lattice and is inhibited by anticancer agents like Taxol. We provide insight into the mechanism of dynamic instability, based on high-resolution cryo-EM structures (4.7-5.6 Å) of dynamic microtubules and microtubules stabilized by GMPCPP or Taxol. We infer that hydrolysis leads to a compaction around the E-site nucleotide at longitudinal interfaces, as well as movement of the α-tubulin intermediate domain and H7 helix. Displacement of the C-terminal helices in both α- and β-tubulin subunits suggests an effect on interactions with binding partners that contact this region. Taxol inhibits most of these conformational changes, allosterically inducing a GMPCPP-like state. Lateral interactions are similar in all conditions we examined, suggesting that microtubule lattice stability is primarily modulated at longitudinal interfaces.

PubMed: 24855948
DOI: 10.1016/j.cell.2014.03.053

Experimental method

ELECTRON MICROSCOPY (4.7 Å)