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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.)

Insights into the structure and function of fungal beta-mannosidases from glycoside hydrolase family 2 based on multiple crystal structures of the Trichoderma harzianum enzyme

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Author(s):
Nascimento, Alessandro S. [1] ; Muniz, Joao Renato C. [1] ; Aparicio, Ricardo [2] ; Golubev, Alexander M. [3] ; Polikarpov, Igor [1]
Total Authors: 5
Affiliation:
[1] Univ Sao Paulo, Inst Fis Sao Carlos, BR-13566590 Sao Carlos, SP - Brazil
[2] Univ Estadual Campinas, Inst Quim, BR-13081970 Campinas, SP - Brazil
[3] Petersburg Nucl Phys Inst, Mol & Radiat Biophys Div, Gatchina, Leningrad Distr - Russia
Total Affiliations: 3
Document type: Journal article
Source: FEBS Journal; v. 281, n. 18, SI, p. 4165-4178, SEP 2014.
Web of Science Citations: 11
Abstract

Hemicellulose is an important part of the plant cell wall biomass, and is relevant to cellulosic ethanol technologies. beta-Mannosidases are enzymes capable of cleaving nonreducing residues of beta-D-mannose from beta-D-mannosides and hemicellulose mannose-containing polysaccharides, such as mannans and galactomannans. beta-Mannosidases are distributed between glycoside hydrolase (GH) families 1, 2, and 5, and only a handful of the enzymes have been structurally characterized to date. The only published X-ray structure of a GH family 2 mannosidase is that of the bacterial Bacteroides thetaiotaomicron enzyme. No structures of eukaryotic mannosidases of this family are currently available. To fill this gap, we set out to solve the structure of Trichoderma harzianum GH family 2 beta-mannosidase and to refine it to 1.9-angstrom resolution. Structural comparisons of the T. harzianum GH2 beta-mannosidase highlight similarities in its structural architecture with other members of GH family 2, reveal the molecular mechanism of beta-mannoside binding and recognition, and shed light on its putative galactomannan-binding site. (AU)

FAPESP's process: 08/56255-9 - Structure and function of enzymes and auxiliary proteins from Trichoderma, active in cell-wall hydrolysis
Grantee:Igor Polikarpov
Support type: Program for Research on Bioenergy (BIOEN) - Thematic Grants
FAPESP's process: 09/52840-7 - Center of Biological and Industrial Processes for Biofuels - CeProBIO
Grantee:Igor Polikarpov
Support type: Program for Research on Bioenergy (BIOEN) - Thematic Grants