Journal
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
Volume 1863, Issue 6, Pages 1015-1026Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbagen.2019.03.013
Keywords
Trichoderma harzianum; GH7; Cellulase; Protein crystallography; Molecular dynamics simulations
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Funding
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [2015/13684-0, 2014/06565-2, 2017/18173-0]
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq) [405191/2015-4, 140667/2015-6, 158752/2015-5, 303988/2016-9, 440977/2016-9]
- Brazilian agency CAPES [A061_2013, 001]
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [14/06565-2, 15/13684-0] Funding Source: FAPESP
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Cellulases from glycoside hydrolase family 7 (GH7) play crucial roles in plant lignocellulose deconstruction by fungi, but structural information available for GH7 fungal endoglucanases is limited when compared to the number of known sequences in the family. Here, we report the X-ray structure of the glycosylated catalytic domain (CD) of Trichoderma harzianwn endoglucanase, ThCel7B, solved and refined at 2.9 angstrom resolution. Additionally, our extensive molecular dynamics simulations of this enzyme in complex with a variety of oligosaccharides provide a better understanding of its promiscuous hydrolytic activities on plant cell wall polysaccharides. The simulations demonstrate the importance of the hydrogen bond between substrate O2 hydroxyl in the subsite - 1 and a side chain of catalytic Glu196 which renders ThCel7B capable to catalytically cleave cello and xylooligosaccharides, but not mannooligosaccharides. Moreover, detailed structural analyses and MD simulations revealed an additional binding pocket, suitable for accommodation of oligosaccharide decorations and/or substrates with mixed glycoside bonds that abuts onto the binding cleft close to subsite +2.
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