Molecular plasticity of CBM3 ancillary domain leads to conformational changes in the cellulose binding interface

Author(s)

Morais, Mariana Abrahao Bueno ; Paiva, Joice Helena ; Murakami, Mario Tyago

• Document type: Journal article
• Source: Biochemical and Biophysical Research Communications; v. 645, p. 8-pg., 2023-01-19.

Abstract

Carbohydrate-binding modules (CBMs) constitute independently folded domains typically associated with carbohydrate-active enzymes (CAZymes). These modules are considered to have a rigid structure without notable conformational changes upon ligand binding, exhibiting a complementary topography in relation to the target carbohydrate. Herein, the high-resolution SAD-solved structure of a CBM from family 3 (BsCBM3) that binds to crystalline cellulose is reported in two crystalline forms. This module showed molecular plasticity with structural differences detected between the two crystalline forms and high RMSD values when compared to NMR ensemble of models. Pronounced structural variances were observed in the cellulose binding interface between NMR and XTAL structures, which were corroborated by molecular dynamics simulations. These findings support that family 3 CBMs targeting to cellulose are rather structurally dynamic modules than rigid entities, suggesting a potential role of conformational changes in polysaccharide recognition and modulation of enzyme activity. (c) 2023 Elsevier Inc. All rights reserved. (AU)

• FAPESP's process: 08/10555-1 - Structural characterization of PthA effector protein from Xanthomonas axonopodis pv. citri, the causal agent of citrus canker
• Grantee: Joice Helena Paiva
• Support Opportunities: Scholarships in Brazil - Doctorate (Direct)
• FAPESP's process: 16/19995-0 - Analysis of structural and functional diversity of GH43 enzymes from Xanthomonas axonopodis pv. citri: biological implications and potential biotechnological applications
• Grantee: Mariana Abrahão Bueno de Morais
• Support Opportunities: Scholarships in Brazil - Post-Doctoral
• FAPESP's process: 15/26982-0 - Exploring novel strategies for depolymerization of plant cell-wall polysaccharides: from structure, function and rational design of glycosyl hydrolases to biological implications and potential biotechnological applications
• Grantee: Mário Tyago Murakami
• Support Opportunities: Research Projects - Thematic Grants