Structure and dynamics of Trichoderma harzianum Cel7B suggest molecular architecture adaptations required for a wide spectrum of activities on plant cell wall polysaccharides

Autor(es)

Sonoda, Milton T. ^[1] ; Godoy, Andre S. ^[2] ; Pellegrini, Vanessa O. A. ^[2] ; Kadowaki, Marco A. S. ^[2] ; Nascimento, Alessandro S. ^[2] ; Polikarpov, Igor ^[2]

Afiliação do(s) autor(es)

^[1] Univ Fed Triangulo Mineiro, Inst Ciencias Exatas Nat & Educ, Dept Fis, Ave Frei Paulino, 30, BR-38025180 Bairro Abadia Uberaba, MG - Brazil

^[2] Univ Sao Paulo, Inst Fis Sao Carlos, Ave Trabalhador Saocarlense, 400, BR-13566590 Sao Carlos, SP - Brazil

• Tipo de documento: Artigo Científico
• Fonte: BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS; v. 1863, n. 6, p. 1015-1026, JUN 2019.
• Citações Web of Science: 5

Resumo

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. (AU)

• Processo FAPESP: 14/06565-2 - Estendendo as fronteiras em interações biomoleculares: docking e avaliação da energia livre
• Beneficiário: Alessandro Silva Nascimento
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 15/13684-0 - Estudos estruturais e funcionais de enzimas que participam na síntese e degradação de carboidratos complexos
• Beneficiário: Igor Polikarpov
• Modalidade de apoio: Auxílio à Pesquisa - Temático
• Processo FAPESP: 17/18173-0 - Mecanismos Envolvidos em Resistência a Antibióticos: Parede de Ácidos Teicóicos e Biofilmes como Alvos Moleculares
• Beneficiário: Alessandro Silva Nascimento
• Modalidade de apoio: Auxílio à Pesquisa - Regular