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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.)

Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism

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Liberato, Marcelo V. [1] ; Silveira, Rodrigo L. [2] ; Prates, Erica T. [2] ; de Araujo, Evandro A. [1] ; Pellegrini, Vanessa O. A. [1] ; Camilo, Cesar M. [1] ; Kadowaki, Marco A. [1] ; Neto, Mario de O. [3] ; Popov, Alexander [4] ; Skaf, Munir S. [2] ; Polikarpov, Igor [1]
Total Authors: 11
[1] Univ Sao Paulo, Sao Carlos Inst Phys, BR-13566590 Sao Paulo - Brazil
[2] Univ Estadual Campinas, Inst Chem, BR-13084862 Sao Paulo - Brazil
[3] State Univ Sao Paulo, Inst Biosci, BR-18618970 Sao Paulo - Brazil
[4] European Synchrotron Radiat Facil, CS40220, Grenoble - France
Total Affiliations: 4
Document type: Journal article
Source: SCIENTIFIC REPORTS; v. 6, APR 1 2016.
Web of Science Citations: 9

Glycoside hydrolases (GHs) play fundamental roles in the decomposition of lignocellulosic biomaterials. Here, we report the full-length structure of a cellulase from Bacillus licheniformis (BlCel5B), a member of the GH5 subfamily 4 that is entirely dependent on its two ancillary modules (Ig-like module and CBM46) for catalytic activity. Using X-ray crystallography, small-angle X-ray scattering and molecular dynamics simulations, we propose that the C-terminal CBM46 caps the distal N-terminal catalytic domain (CD) to establish a fully functional active site via a combination of large-scale multidomain conformational selection and induced-fit mechanisms. The Ig-like module is pivoting the packing and unpacking motions of CBM46 relative to CD in the assembly of the binding subsite. This is the first example of a multidomain GH relying on large amplitude motions of the CBM46 for assembly of the catalytically competent form of the enzyme. (AU)

FAPESP's process: 10/18773-8 - Molecular cloning, expression, purification and structural characterization of endoglucanase from Trichoderma harzianum aiming the development of enzymatic blends for production of lignocellulosic ethanol
Grantee:Vanessa de Oliveira Arnoldi Pellegrini
Support type: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 13/08293-7 - CCES - Center for Computational Engineering and Sciences
Grantee:Munir Salomao Skaf
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 13/15582-5 - Multiscale molecular dynamics of glycoside hydrolases and lignocellulosic substrates
Grantee:Érica Teixeira Prates
Support type: Scholarships in Brazil - Post-Doctorate
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
FAPESP's process: 14/10448-1 - Molecular aspects of plant cell wall architecture
Grantee:Rodrigo Leandro Silveira
Support type: Scholarships in Brazil - Post-Doctorate
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