4U3J: TOG2:alpha/beta-tubulin complex

Stu2p/XMAP215 proteins are essential microtubule polymerases that use multiple alphabeta-tubulin-interacting TOG domains to bind microtubule plus ends and catalyze fast microtubule growth. We report here the structure of the TOG2 domain from Stu2p bound to yeast alphabeta-tubulin. Like TOG1, TOG2 binds selectively to a fully 'curved' conformation of alphabeta-tubulin, incompatible with a microtubule lattice. We also show that TOG1-TOG2 binds non-cooperatively to two alphabeta-tubulins. Preferential interactions between TOGs and fully curved alphabeta-tubulin that cannot exist elsewhere in the microtubule explain how these polymerases localize to the extreme microtubule end. We propose that these polymerases promote elongation because their linked TOG domains concentrate unpolymerized alphabeta-tubulin near curved subunits already bound at the microtubule end. This tethering model can explain catalyst-like behavior and also predicts that the polymerase action changes the configuration of the microtubule end.
PDB ID: 4U3JDownload
MMDB ID: 122614
PDB Deposition Date: 2014/7/22
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 2.81  Å
Source Organism:
Similar Structures:
Biological Unit for 4U3J: trimeric; determined by author
Molecular Components in 4U3J
Label Count Molecule
Proteins (3 molecules)
Tubulin Alpha-1 Chain(Gene symbol: TUB1)
Molecule annotation
Tubulin Beta Chain(Gene symbol: TUB2)
Molecule annotation
Protein Stu2(Gene symbol: STU2)
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB