title: Promiscuous interactions of human septins: the GTP binding domain of SEPT7 forms filaments within the crystal.
abstract: We describe the purification, crystallization and structure for the GTP-binding domain of human septin 7 (SEPT7G). We show that it forms filaments within the crystal lattice which employ both the G and NC interfaces, similar to those seen in the hetero-filament of SEPT2/6/7. The NC interface is considered promiscuous as it is absent from the hetero-filament. Such promiscuity could provide the potential for permuting monomers along a filament in order to generate diversity in hetero-polymers. On the other hand, our results suggest that the G and NC interfaces may be necessary but insufficient for determining correct hetero-filament assembly.
authors: Centro de Biotecnologia Molecular Estrutural, Instituto de Física de São Carlos, Universidade de São Paulo, São Carlos, SP, Brazil.
authors: Vitor Hugo Balasco
authors: VH
authors: Serrão
authors: Fernando
authors: F
authors: Alessandro
authors: Victor Emanoel Armini
authors: VE
authors: Caldas
authors: Rafaela Leite
authors: RL
authors: Marçal
authors: Humberto D'Muniz
authors: HD
authors: Pereira
authors: Otavio Henrique
authors: OH
authors: Thiemann
authors: Richard Charles
authors: RC
authors: Garratt
mesh_terms: D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D018360:Crystallography, X-Ray; D006160:Guanosine Triphosphate / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D058112:Septins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D018797:Cell Cycle Proteins; D021122:Protein Subunits; D006160:Guanosine Triphosphate; C113158:SEPTIN7 protein, human; D058112:Septins