| Texto completo | |
| Autor(es): Mostrar menos - |
Santos, Camila R.
[1]
;
Costa, Pedro A. C. R.
[2, 1]
;
Vieira, Plinio S.
[1]
;
Gonzalez, Sinkler E. T.
[3]
;
Correa, Thamy L. R.
[1]
;
Lima, Evandro A.
[1]
;
Mandelli, Fernanda
[1]
;
Pirolla, Renan A. S.
[1]
;
Domingues, Mariane N.
[1]
;
Cabral, Lucelia
[1]
;
Martins, Marcele P.
[1]
;
Cordeiro, Rosa L.
[1]
;
Junior, Atilio T.
[1]
;
Souza, Beatriz P.
[1]
;
Prates, Erica T.
[3, 4]
;
Gozzo, Fabio C.
[3]
;
Persinoti, Gabriela F.
[1]
;
Skaf, Munir S.
[3]
;
Murakami, Mario T.
[1]
Número total de Autores: 19
|
| Afiliação do(s) autor(es): | [1] Brazilian Ctr Res Energy & Mat, Brazilian Biorenewables Natl Lab, Campinas, SP - Brazil
[2] Univ Estadual Campinas, Inst Biol, Grad Program Funct & Mol Biol, Campinas, SP - Brazil
[3] Univ Estadual Campinas, Inst Chem, Campinas, SP - Brazil
[4] Oak Ridge Natl Lab, Biosci Div, Oak Ridge, TN - USA
Número total de Afiliações: 4
|
| Tipo de documento: | Artigo Científico |
| Fonte: | Nature Chemical Biology; v. 16, n. 8 MAY 2020. |
| Citações Web of Science: | 1 |
| Resumo | |
Comprehensive informatic, structural and biochemical characterization of the GH128 family defines subgroups of glycoside hydrolase enzymes with unique recognition and cleavage mechanisms for 1,3-beta-glucan polysaccharide substrates. The fundamental and assorted roles of beta-1,3-glucans in nature are underpinned on diverse chemistry and molecular structures, demanding sophisticated and intricate enzymatic systems for their processing. In this work, the selectivity and modes of action of a glycoside hydrolase family active on beta-1,3-glucans were systematically investigated combining sequence similarity network, phylogeny, X-ray crystallography, enzyme kinetics, mutagenesis and molecular dynamics. This family exhibits a minimalist and versatile (alpha/beta)-barrel scaffold, which can harbor distinguishing exo or endo modes of action, including an ancillary-binding site for the anchoring of triple-helical beta-1,3-glucans. The substrate binding occurs via a hydrophobic knuckle complementary to the canonical curved conformation of beta-1,3-glucans or through a substrate conformational change imposed by the active-site topology of some fungal enzymes. Together, these findings expand our understanding of the enzymatic arsenal of bacteria and fungi for the breakdown and modification of beta-1,3-glucans, which can be exploited for biotechnological applications. (AU) | |
| Processo FAPESP: | 13/08293-7 - CECC - Centro de Engenharia e Ciências Computacionais |
| Beneficiário: | Munir Salomao Skaf |
| Modalidade de apoio: | Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs |
| Processo FAPESP: | 15/26982-0 - Explorando novas estratégias para a despolimerização de polissacarídeos da parede celular vegetal: da estrutura, função e desenho racional de hidrolases glicosídicas às implicações biológicas e potenciais aplicações biotecnológicas |
| Beneficiário: | Mário Tyago Murakami |
| Modalidade de apoio: | Auxílio à Pesquisa - Temático |