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

Santos, Camila R.; Costa, Pedro A.  C.  R.; Vieira, Plínio S.; Gonzalez, Sinkler E. T.; Correa, Thamy L.  R.; Lima, Evandro A.; Mandelli, Fernanda; Pirolla, Renan A. S.; Domingues, Mariane N.; Cabral, Lucelia; Martins, Marcele P.; Cordeiro, Rosa L.; Junior, Atílio T.; Souza, Beatriz P.; Prates, Érica T.; Gozzo, Fabio C.; Persinoti, Gabriela F.; Skaf, Munir S.; Murakami, Mario T.

doi:10.1038/s41589-020-0554-5

Title: Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family

Journal Article · Mon May 25 00:00:00 EDT 2020 · Nature Chemical Biology

DOI:https://doi.org/10.1038/s41589-020-0554-5· OSTI ID:1633140

^[1]; Costa, Pedro A. C. R. ^[2];

^[1]; Gonzalez, Sinkler E. T. ^[3]; Correa, Thamy L. R. ^[1]; Lima, Evandro A. ^[1]; Mandelli, Fernanda ^[1];

^[1]; Domingues, Mariane N. ^[1]; Cabral, Lucelia ^[1]; Martins, Marcele P. ^[1]; Cordeiro, Rosa L. ^[1]; Junior, Atílio T. ^[1]; Souza, Beatriz P. ^[1]; Prates, Érica T. ^[3]; Gozzo, Fabio C. ^[3];

^[1]; Skaf, Munir S. ^[3];

^[1]

Brazilian Center for Research in Energy and Materials, Campinas, São Paulo (Brazil)
Brazilian Center for Research in Energy and Materials, Campinas, São Paulo (Brazil); Univ. of Campinas (UNICAMP), São Paulo (Brazil)
Univ. of Campinas (UNICAMP), São Paulo (Brazil)

The fundamental and assorted roles of β-1,3-glucans in nature are underpinned on diverse chemistry and molecular structures, demanding sophisticated and intricate enzymatic systems for their processing. Herein, the selectivity and modes of action of a glycoside hydrolase family active on β-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 (α/β)-barrel scaffold, which can harbor distinguishing exo or endo modes of action, including an ancillary-binding site for the anchoring of triple-helical β-1,3-glucans. The substrate binding occurs via a hydrophobic knuckle complementary to the canonical curved conformation of β-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 β-1,3-glucans, which can be exploited for biotechnological applications.

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Research Organization:: Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER); National Institutes of Health (NIH); National Institute of General Medical Sciences (NIGMS); Fundação de Amparo a Pesquisa do Estado de São Paulo (FAPESP); Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Grant/Contract Number:: AC05-00OR22725; AC02-76SF00515; 2015/26982-0; 2013/08293-7; 306135/2016-7

OSTI ID:: 1633140

Journal Information:: Nature Chemical Biology, Vol. 16, Issue 8; ISSN 1552-4450

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 11 works

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