Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/337658
Type: Artigo
Title: Crystallographic structure and molecular dynamics simulations of the major endoglucanase from Xanthomonas campestris pv. campestris shed light on its oligosaccharide products release pattern
Author: Puhl, Ana C.
Prates, Erica T.
Rosseto, Flávio R.
Manzine, Livia R.
Stankovic, Ivana
Araújo, Simara S. de
Alvarez, Thabata M.
Squina, Fábio M.
Skaf, Munir S.
Polikarpov, Igor
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 β-1,3 and β-1,4 bonds within the binding cleft which are related to the enzymatic efficiency
Subject: Endoglucanases
Dinâmica molecular
Country: Países Baixos
Editor: Elsevier
Rights: Fechado
Identifier DOI: 10.1016/j.ijbiomac.2019.06.107
Address: https://www.sciencedirect.com/science/article/pii/S0141813019301278
Date Issue: Sep-2019
Appears in Collections:IQ - Artigos e Outros Documentos

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