Crystal structure of a Schistosoma mansoni septin reveals the phenomenon of strand slippage in septins dependent on the nature of the bound nucleotide.

@article{Zeraik2014CrystalSO,
  title={Crystal structure of a Schistosoma mansoni septin reveals the phenomenon of strand slippage in septins dependent on the nature of the bound nucleotide.},
  author={Ana Eliza Zeraik and Humberto D’Muniz Pereira and Yuri D. Santos and Jos{\'e} Brand{\~a}o-Neto and Michael Spoerner and Maiara S. Santos and Luiz Alberto Colnago and Richard Garratt and Ana P U Araujo and Ricardo DeMarco},
  journal={The Journal of biological chemistry},
  year={2014},
  volume={289 11},
  pages={7799-811}
}
Septins are filament-forming GTP-binding proteins involved in important cellular events, such as cytokinesis, barrier formation, and membrane remodeling. Here, we present two crystal structures of the GTPase domain of a Schistosoma mansoni septin (SmSEPT10), one bound to GDP and the other to GTP. The structures have been solved at an unprecedented resolution for septins (1.93 and 2.1 Å, respectively), which has allowed for unambiguous structural assignment of regions previously poorly defined… CONTINUE READING
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