Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering

Autor(es)

Seraphim, Thiago V. ; Silva, Kelly P. ; Dores-Silva, Paulo R. ; Barbosa, Leandro R. S. ; Borges, Julio C.

• Tipo de documento: Artigo Científico
• Fonte: International Journal of Biological Macromolecules; v. 97, p. 503-512, APR 2017.
• Citações Web of Science: 6

Resumo

Heat shock protein of 90 kDa (Hsp90) is an essential molecular chaperone involved in a plethora of cellular activities which modulate protein homeostasis. During the Hsp90 mechanochemical cycle, it undergoes large conformational changes, oscillating between open and closed states. Although structural and conformational equilibria of prokaryotic and some eukaryotic Hsp90s are known, some protozoa Hsp90 structures and dynamics are poorly understood. In this study, we report the solution structure and conformational dynamics of Leishmania braziliensis Hsp90 (LbHsp90) investigated by small angle X-ray scattering (SAXS). The results indicate that LbHsp90 coexists in open and closed conformations in solution and that the linkers between domains are not randomly distributed. These findings noted interesting features of the LbHsp90 system, opening doors for further conformational studies of other protozoa chaperones. (C) 2017 Elsevier B.V. All rights reserved. (AU)

• Processo FAPESP: 14/07206-6 - Estudos da HSP70 mitocondrial de humanos e de protozoários: abordagem estrutural e funcional
• Beneficiário: Julio Cesar Borges
• Linha de fomento: Auxílio à Pesquisa - Regular
• Processo FAPESP: 12/50161-8 - Estudo da estrutura e função da chaperona Hsp90 com ênfase no seu papel em homeostase celular
• Beneficiário: Carlos Henrique Inacio Ramos
• Linha de fomento: Auxílio à Pesquisa - Temático
• Processo FAPESP: 11/23110-0 - Uso da calorimetria de titulação isotérmica para a determinação de propriedades termodinâmicas de interação de proteína-ligante e proteína-proteína
• Beneficiário: Julio Cesar Borges
• Linha de fomento: Auxílio à Pesquisa - Regular