| Texto completo | |
| Autor(es): |
Zeraik, Ana E.
[1]
;
Pereira, Humberto M.
[1]
;
Santos, Yuri V.
[1]
;
Brandao-Neto, Jose
[2]
;
Spoerner, Michael
[3]
;
Santos, Maiara S.
[4, 5]
;
Colnago, Luiz A.
[5]
;
Garratt, Richard C.
[1]
;
Araujo, Ana P. U.
[1]
;
DeMarco, Ricardo
[1]
Número total de Autores: 10
|
| Afiliação do(s) autor(es): | [1] Univ Sao Paulo, Inst Fis Sao Carlos, BR-13563120 Sao Carlos, SP - Brazil
[2] Diamond Light Source, Didcot OX11 0DE, Oxon - England
[3] Univ Regensburg, Ctr Magnet Resonance Chem & Biomed, Inst Biophys & Phys Biochem, D-93053 Regensburg - Germany
[4] Univ Sao Paulo, Inst Quim Sao Carlos, BR-13566590 Sao Carlos, SP - Brazil
[5] Embrapa Instrumentacao, BR-13560970 Sao Carlos, SP - Brazil
Número total de Afiliações: 5
|
| Tipo de documento: | Artigo Científico |
| Fonte: | Journal of Biological Chemistry; v. 289, n. 11, p. 7799-7811, MAR 14 2014. |
| Citações Web of Science: | 16 |
| Resumo | |
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. Septins are filament-forming GTP-binding proteins involved in important cellular events, such as cytokinesis, barrier formation, and membrane remodeling. Here, we present two crystal structures of the GTPase domain of a Schistosoma mansoni septin (SmSEPT10), one bound to GDP and the other to GTP. The structures have been solved at an unprecedented resolution for septins (1.93 and 2.1 , respectively), which has allowed for unambiguous structural assignment of regions previously poorly defined. Consequently, we provide a reliable model for functional interpretation and a solid foundation for future structural studies. Upon comparing the two complexes, we observe for the first time the phenomenon of a strand slippage in septins. Such slippage generates a front-back communication mechanism between the G and NC interfaces. These data provide a novel mechanistic framework for the influence of nucleotide binding to the GTPase domain, opening new possibilities for the study of the dynamics of septin filaments. (AU) | |
| Processo FAPESP: | 08/57910-0 - Instituto Nacional de Biotecnologia Estrutural e Química Medicinal em Doenças Infecciosas - INBEQMeDI |
| Beneficiário: | Richard Charles Garratt |
| Modalidade de apoio: | Auxílio à Pesquisa - Temático |