Advanced search
Start date
Betweenand
(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

Full text
Author(s):
Show less -
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
Affiliation:
[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
Abstract

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