@article{
author = "Puhl, Ana C. and Prates, Erica T. and Rosseto, Flávio R. and Manzine, Livia R. and Stanković, Ivana and de Araújo, Simara S. and Alvarez, Thabata M. and Squina, Fábio M. and Skaf, Munir S. and Polikarpov, Igor",
year = "2019",
abstract = "Cellulases are essential enzymatic components for the transformation of plant biomass into fuels, renewable ma-
terials 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.",
publisher = "Elsevier B.V.",
journal = "International Journal of Biological Macromolecules",
title = "Crystallographic structure and molecular dynamics simulations of the major endoglucanase from Xanthomonas campestris pv. campestris shed light on its oligosaccharide products release pattern",
volume = "136",
pages = "493-502",
doi = "10.1016/j.ijbiomac.2019.06.107"
}