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Publication Abstract from PubMed

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 A respectively) which has allowed for unambiguous structural assignment of regions previously poorly defined. Consequently we provide a reliable model for functional interpretation and a solid foundation for future structural studies. On comparing the two complexes, we observe for the first time the phenomenon of a strand slippage in septins. Such slippage generates a front-back communication mechanism between the G and NC interfaces. This data provides a novel mechanistic framework for the influence of nucleotide binding to the GTPase domain, opening new possibilities for the study of the dynamics of septin filaments.

Crystal structure of a Schistosoma mansoni septin reveals the phenomenon of strand slippage in septins dependent on the nature of the bound nucleotide.,Zeraik AE, Pereira HM, Santos YV, Brandao-Neto J, Spoerner M, Santos MS, Colnago LA, Garratt RC, Araujo AP, Demarco R J Biol Chem. 2014 Jan 24. PMID:24464615^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.