| Texto completo | |
| Autor(es): |
Silva, Sergio Bergamachi
;
Pinheiro, Matheus Pinto
;
Fuzo, Carlos Alessandro
;
Silva, Samuel Reghim
;
Ferreira, Tatiane Lopes
;
Lourenzoni, Marcos Roberto
;
Nonato, M. Cristina
;
Vieira, Davi Serradella
;
Ward, Richard John
Número total de Autores: 9
|
| Tipo de documento: | Artigo Científico |
| Fonte: | International Journal of Biological Macromolecules; v. 97, p. 574-584, APR 2017. |
| Citações Web of Science: | 2 |
| Resumo | |
A thermostable variant of the mesophilic xylanase A from Bacillus subtilis (BsXynA-G3\_4x) contains the four mutations Gln7His, Gly13Arg, Ser22Pro, and Ser179Cys. The crystal structure of the BsXynA-G3\_4x has been solved, and the local environments around each of these positions investigated by molecular dynamics (MD) simulations at 328 K and 348 K. The structural and MD simulation results were correlated with thermodynamic data of the wild-type enzyme, the 4 single mutants and the BsXynA-G3\_4x. This analysis suggests that the overall stabilizing effect is entropic, and is consistent with solvation of charged residues and reduction of main-chain flexibility. Furthermore, increased protein-protein hydrogen bonding and hydrophobic interactions also contribute to stabilize the BsXynA-G3\_4x. The study revealed that a combination of several factors is responsible for increased thermostability of the BsXynA-G3\_4x; (i) introduction of backbone rigidity in regions of high flexibility, (ii) solvation effects and (iii) hydrophobic contacts. (C) 2017 Elsevier B.V. All rights reserved. (AU) | |
| Processo FAPESP: | 10/18850-2 - Identificação, caracterização e engenharia de enzimas que degradam a parede celular das plantas |
| Beneficiário: | Richard John Ward |
| Modalidade de apoio: | Auxílio à Pesquisa - Temático |
| Processo FAPESP: | 09/50838-5 - Determinantes de estabilidade estrutural de enzimas xilanases termofílicas mutantes por dinâmica molecular: efeitos da glicosilação sobre a termoestabilidade |
| Beneficiário: | Davi Serradella Vieira |
| Modalidade de apoio: | Bolsas no Brasil - Pós-Doutorado |
| Processo FAPESP: | 12/01066-2 - Desenho de enzimas multifuncionais que combinam a hidrólise de B-Glucanos e xilanos para avaliação da conformação destes polissacarídeos na parede celular de plantas |
| Beneficiário: | Matheus Pinto Pinheiro |
| Modalidade de apoio: | Bolsas no Brasil - Pós-Doutorado |