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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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Structural and biochemical properties of Sept7, a unique septin required for filament formation

Eldar Zent1 / Ingrid Vetter1 / 1

1Structural Biology Group, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 14, D-44227 Dortmund, Germany

Corresponding author

Citation Information: Biological Chemistry. Volume 392, Issue 8-9, Pages 791–797, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2011.082, August 2011

Publication History



Septins constitute a family of conserved guanine nucleotide binding proteins found in a wide range of organisms from fungi to mammals. Members of the family share a canonical G-domain with N- and C-terminal extensions. G-domains assemble into hetero-oligomeric complexes which form non-polarised filaments or rings. Linear filaments are formed between the G-domains using either the guanine nucleotide binding site (G interface) or N- and C-terminal extensions (NC interface). Sept7 is a unique among the 13 human septins in that it occupies the ends of hexameric building blocks which assemble into non-polarised filaments. To gain insight into its particular properties we performed structural and biochemical studies on Sept7. We solved the crystal structure of a Sept7 dimer in the GDP-bound state. The structure and biochemistry of Sept7 provide new insights into the dynamics of the G interface and outline the differences in the properties of Sept7 compared to the members of group 2 septins.

Keywords: cytoskeleton; filament; GTP-binding protein; septin; X-ray crystallography

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