Zeraik, Ana E. and Pereira, Humberto M. and Santos, Yuri V. and Brandao-Neto, Jose and Spoerner, Michael and Santos, Maiara S. and Colnago, Luiz A. and Garratt, Richard C. and Araujo, Ana P. U. and DeMarco, Ricardo (2014) Crystal Structure of a Schistosoma mansoni Septin Reveals the Phenomenon of Strand Slippage in Septins Dependent on the Nature of the Bound Nucleotide. JOURNAL OF BIOLOGICAL CHEMISTRY, 289 (11). pp. 7799-7811. ISSN 0021-9258, 1083-351X
Full text not available from this repository. (Request a copy)Abstract
Background: Septins are filament-forming proteins involved in membrane-remodeling events. Results: Two crystal structures of a septin with the highest resolution to date reveal the phenomenon of -strand slippage. Conclusion: A novel mechanistic framework for the influence of the nature of the bound nucleotide and the presence of Mg2+ in septins is proposed. Significance: Identification of strand slippage might contribute to elucidating the mechanism of septin association with membranes. 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 , 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. Upon 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. These data provide 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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | FILAMENT FORMATION; MAMMALIAN SEPTINS; GTP-BINDING; FORMS FILAMENTS; YEAST SEPTIN; ARF; HYDROLYSIS; COMPLEXES; PROTEINS; FAMILY; Crystal Structure; GTPase; Protein Conformation; Protein Structure; X-ray Crystallography; Conformational Change; Filament; GTPase Domain; Schistosoma; Septin |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 18 Nov 2019 08:32 |
| Last Modified: | 18 Nov 2019 08:32 |
| URI: | https://pred.uni-regensburg.de/id/eprint/10469 |
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