3T5D

Crystal structure of Septin 7 in complex with GDP

Summary for 3T5D

• Entry DOI: 10.2210/pdb3t5d/pdb
• Descriptor: Septin-7, GUANOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: gtp-binding protein, cytoskeleton, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q16181
• Total number of polymer chains: 2
• Total formula weight: 63586.20

Authors

Zent, E.,Wittinghofer, A. (deposition date: 2011-07-27, release date: 2011-08-24, Last modification date: 2024-02-28)

Primary citation

Zent, E.,Vetter, I.,Wittinghofer, A.
Structural and biochemical properties of Sept7, a unique septin required for filament formation.
Biol.Chem., 392:791-797, 2011

PubMed Abstract: 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.

PubMed: 21824007
DOI: 10.1515/BC.2011.082

Experimental method

X-RAY DIFFRACTION (3.3 Å)