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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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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]
Total Authors: 19
[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
Total Affiliations: 4
Document type: Journal article
Source: Nature Chemical Biology; v. 16, n. 8 MAY 2020.
Web of Science Citations: 1

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)

FAPESP's process: 13/08293-7 - CCES - Center for Computational Engineering and Sciences
Grantee:Munir Salomao Skaf
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 15/26982-0 - Exploring novel strategies for depolymerization of plant cell-wall polysaccharides: from structure, function and rational design of glycosyl hydrolases to biological implications and potential biotechnological applications
Grantee:Mário Tyago Murakami
Support type: Research Projects - Thematic Grants