Promiscuous interactions of human septins: The GTP binding domain of SEPT7 forms filaments within the crystal

Author(s)

Balasco Serrao, Vitor Hugo ; Alessandro, Fernando ; Armini Caldas, Victor Emanoel ; Marcal, Rafaela Leite ; Pereira, Humberto D'Muniz ; Thiemann, Otavio Henrique ; Garratt, Richard Charles ^[1]

Affiliation

^[1] Univ Sao Paulo, Inst Fis Sao Carlos, Dept Fis & Informat, Ctr Biotecnol Mol Estrutural, BR-13560970 Sao Carlos, SP - Brazil

• Document type: Journal article
• Source: FEBS Letters; v. 585, n. 24, p. 3868-3873, DEC 15 2011.
• Web of Science Citations: 14

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 heteropolymers. On the other hand, our results suggest that the G and NC interfaces may be necessary but insufficient for determining correct hetero-filament assembly. Structured summary of protein interactions: SEPT7G and SEPT7G bind by X-ray crystallography (View interaction). SEPT7 G and SEPT7 G bind by molecular sieving (View interaction). (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved. (AU)

• FAPESP's process: 08/57910-0 - National Institute of Structural Biotechnology and Medicinal Chemistry in Infectious Diseases
• Grantee: Richard Charles Garratt
• Support Opportunities: Research Projects - Thematic Grants
• FAPESP's process: 98/14138-2 - Center for Structural Molecular Biotechnology
• Grantee: Glaucius Oliva
• Support Opportunities: Research Grants - Research, Innovation and Dissemination Centers - RIDC