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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.)

Crystallographic structure and molecular dynamics simulations of the major endoglucanase from Xanthomonas campestris pv. campestris shed light on its oligosaccharide products release pattern

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Author(s):
Puhl, Ana C. [1] ; Prates, Erica T. [2, 3] ; Rosseto, Flavio R. [1] ; Manzine, Livia R. [1] ; Stankovic, Ivana [2] ; de Araujo, Simara S. [1] ; Alvarez, Thabata M. [4] ; Squina, Fabio M. [4] ; Skaf, Munir S. [2] ; Polikarpov, Igor [1]
Total Authors: 10
Affiliation:
[1] Univ Soo Paulo, Inst Fis Sao Carlos, Av Trabalhador Sao Carlense 400, BR-13560970 Sao Carlos, SP - Brazil
[2] Univ Estadual Campinas, Inst Quim, UNICAMP, Cx P 6154, BR-13082086 Campinas, SP - Brazil
[3] Oak Ridge Natl Lab, Biosci Div, POB 2009, Oak Ridge, TN 37830 - USA
[4] Univ Sorocaba UNISO, Programa Proc Tecnol & Ambientais, Sorocaba, SP - Brazil
Total Affiliations: 4
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 136, p. 493-502, SEP 1 2019.
Web of Science Citations: 0
Abstract

Cellulases are essential enzymatic components for the transformation of plant biomass into fuels, renewable materials and green chemicals. Here, we determined the crystal structure, pattern of hydrolysis products release, and conducted molecular dynamics simulations of the major endoglucanase from the Xanthomonas campestris pv. campestris (XccCel5A). XccCel5A has a TIM barrel fold with the catalytic site centrally placed in a binding groove surrounded by aromatic side chains. Molecular dynamics simulations show that productive position of the substrate is secured by a network of hydrogen bonds in the four main subsites, which differ in details from homologous structures. Capillary zone electrophoresis and computational studies reveal XccCel5A can act both as endoglucanase and licheninase, but there are preferable arrangements of substrate regarding beta-1,3 and beta-1,4 bonds within the binding cleft which are related to the enzymatic efficiency. (C) 2019 Published by Elsevier B.V. (AU)

FAPESP's process: 11/20505-4 - Two important classes of glycosyl hydrolases: functional studies and structural analysis
Grantee:Marco Antonio Seiki Kadowaki
Support Opportunities: Scholarships in Brazil - Post-Doctoral
FAPESP's process: 15/13684-0 - Structural and functional studies of enzymes that participate in complex carbohydrates synthesis and degradation
Grantee:Igor Polikarpov
Support Opportunities: Research Projects - Thematic Grants
FAPESP's process: 09/52840-7 - Center of Biological and Industrial Processes for Biofuels - CeProBIO
Grantee:Igor Polikarpov
Support Opportunities: Program for Research on Bioenergy (BIOEN) - Thematic Grants
FAPESP's process: 10/52362-5 - Targeted analysis of microbial lignocellulolytic secretomes: a new approach to enzyme discovery
Grantee:Igor Polikarpov
Support Opportunities: Regular Research Grants
FAPESP's process: 11/21608-1 - Identification and characterization of new enzymes with potential for lignocellulosic biomass conversion
Grantee:Bruno Luan Soares Paula de Mello
Support Opportunities: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 15/50590-4 - Lignin valorization in cellulosic ethanol plants: biocatalytic conversion via ferulic acid to high value chemicals
Grantee:Fábio Márcio Squina
Support Opportunities: Program for Research on Bioenergy (BIOEN) - Thematic Grants