4u3j
From Proteopedia
TOG2:alpha/beta-tubulin complex
Structural highlights
Function[TBA1_YEAST] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. [STU2_YEAST] May play a role in the attachment, organization, and/or dynamics of microtubule ends at the spindle pole body. [TBB_YEAST] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. Publication Abstract from PubMedStu2p/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. A tethered delivery mechanism explains the catalytic action of a microtubule polymerase.,Ayaz P, Munyoki S, Geyer EA, Piedra FA, Vu ES, Bromberg R, Otwinowski Z, Grishin NV, Brautigam CA, Rice LM Elife. 2014 Aug 5:e03069. doi: 10.7554/eLife.03069. PMID:25097237[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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