| Full text | |
| Author(s): |
Nascimento, Alessandro S.
;
Muniz, Joao Renato C.
;
Aparicio, Ricardo
;
Golubev, Alexander M.
;
Polikarpov, Igor
Total Authors: 5
|
| Document type: | Journal article |
| Source: | FEBS Journal; v. 281, n. 18, p. 14-pg., 2014-09-01. |
| 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: | 09/52840-7 - Center of Biological and Industrial Processes for Biofuels - CeProBIO |
| Grantee: | Igor Polikarpov |
| Support Opportunities: | Program for Research on Bioenergy (BIOEN) - Thematic Grants |
| 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 Opportunities: | Program for Research on Bioenergy (BIOEN) - Thematic Grants |