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Crystal Structure of a Schistosoma mansoni Septin Reveals the Phenomenon of Strand Slippage in Septins Dependent on the Nature of the Bound Nucleotide

DOI: 10.1074/jbc.M113.525352 DOI Help
PMID: 24464615 PMID Help

Authors: A. E. Zeraik (São Carlos Institute of Physics, University of São Paulo) , H. M. Pereira (São Carlos Institute of Physics, University of São Paulo) , Y. V. Santos (São Carlos Institute of Physics, University of São Paulo) , J. Brandao-neto (Diamond Light Source) , M. Spoerner (Centre of Magnetic Resonance in Chemistry and Biomedicine (CMRCB), University of Regensburg,) , M. S. Santos (University of São Paulo) , L. A. Colnago (University of São Paulo) , R. C. Garratt (São Carlos Institute of Physics, University of São Paulo) , A. P. U. Araujo (São Carlos Institute of Physics, University of São Paulo) , R. Demarco (São Carlos Institute of Physics, University of São Paulo)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Biological Chemistry , VOL 289 (11) , PAGES 7799 - 7811

State: Published (Approved)
Published: January 2014

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.

Journal Keywords: Binding; Calorimetry; Catalysis; Cell; Crystallography; X-Ray; Escherichia; GTP; Guanosine; Guanosine; Hydrolysis; Magnesium; Magnetic; Nucleotides; Protein; Secondary; Protein; Tertiary; Recombinant; Schistosoma; Septins; Thermodynamics; Water

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I24-Microfocus Macromolecular Crystallography