Structural insights into beta-1,3-glucan cleavage by a glycoside hydrolase family

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]

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

• 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