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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Exploring the Molecular Basis for Substrate Affinity and Structural Stability in Bacterial GH39 beta-Xylosidases

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de Morais, Mariana Abrahao Bueno [1] ; Polo, Carla Cristina [2] ; Domingues, Mariane Noronha [1] ; Persinoti, Gabriela Felix [1] ; Pirolla, Renan Augusto Siqueira [1] ; de Souza, Flavio Henrique Moreira [1] ; Correa, Jessica Batista de Lima [1] ; dos Santos, Camila Ramos [1] ; Murakami, Mario Tyago [1]
Total Authors: 9
[1] Brazilian Ctr Res Energy & Mat, Brazilian Biorenewables Natl Lab, Campinas - Brazil
[2] Brazilian Ctr Res Energy & Mat, Brazilian Synchrotron Light Lab, Campinas - Brazil
Total Affiliations: 2
Document type: Journal article
Web of Science Citations: 0

The glycoside hydrolase family 39 (GH39) is a functionally expanding family with limited understanding about the molecular basis for substrate specificity and extremophilicity. In this work, we demonstrate the key role of the positive-subsite region in modulating substrate affinity and how the lack of a C-terminal extension impacts on oligomerization and structural stability of some GH39 members. The crystallographic and SAXS structures of a new GH39 member from the phytopathogen Xanthomonas citri support the importance of an extended C-terminal to promote oligomerization as a molecular strategy to enhance thermal stability. Comparative structural analysis along with site-directed mutagenesis showed that two residues located at the positive-subsite region, Lys166 and Asp167, are critical to substrate affinity and catalytic performance, by inducing local changes in the active site for substrate binding. These findings expand the molecular understanding of the mechanisms involved in substrate recognition and structural stability of the GH39 family, which might be instrumental for biological insights, rational enzyme engineering and utilization in biorefineries. (AU)

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 type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 13/24622-0 - Elucidation of the mechanistic basis of family GH62 present in organisms specialized in the degradation of plant biomass
Grantee:Flavio Henrique Moreira de Souza
Support type: Scholarships in Brazil - Post-Doctorate
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 type: Research Projects - Thematic Grants