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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.)

High-resolution structure of a modular hyperthermostable endo-beta-1,4-mannanase from Thermotoga petrophila: The ancillary immunoglobulin-like module is a thermostabilizing domain

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Author(s):
da Silva, Viviam M. [1, 2] ; Cabral, Aline D. [3] ; Speranca, Marcia A. [3] ; Squina, Fabio M. [4] ; Muniz, Joao Renato C. [5] ; Martin, Lydie [2] ; Nicolet, Yvain [2] ; Garcia, Wanius [1]
Total Authors: 8
Affiliation:
[1] Univ Fed ABC UFABC, Ctr Ciencias Nat & Humanas, Santo Andre, SP - Brazil
[2] Univ Grenoble Alpes, CEA, CNRS, IBS, Metalloprot Unit, F-38000 Grenoble - France
[3] Univ Fed ABC UFABC, Ctr Ciencias Nat & Humanas, Sao Bernardo Do Campo, SP - Brazil
[4] Univ Sorocaba UNISO, Programa Proc Tecnol & Ambientais, Sorocaba, SP - Brazil
[5] Univ Sao Paulo, Sao Carlos Inst Phys IFSC, Sao Carlos, SP - Brazil
Total Affiliations: 5
Document type: Journal article
Source: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS; v. 1868, n. 8 AUG 2020.
Web of Science Citations: 0
Abstract

The endo-beta-1,4-mannanase from the hyperthermostable bacterium Thermotoga petrophila (TpMan) is an enzyme that catalyzes the hydrolysis of mannan and heteromannan polysaccharides. Of the three domains that comprise TpMan, the N-terminal GH5 catalytic domain and the C-terminal carbohydrate-binding domain are connected through a central ancillary domain of unknown structure and function. In this study, we report the partial crystal structure of the TpMan at 1.45 angstrom resolution, so far, the first modular hyperthermostable endo-beta-1,4-mannanase structure determined. The structure exhibits two domains, a (beta/alpha)(8)-barrel GH5 catalytic domain connected via a linker to the central domain with an immunoglobulin-like beta-sandwich fold formed of seven beta-strands. Functional analysis showed that whereas the immunoglobulin-like domain does not have the carbohydrate-binding function, it stacks on the GH5 catalytic domain acting as a thermostabilizing domain and allowing operation at hyperthermophilic conditions. The carbohydrate-binding domain is absent in the crystal structure most likely due to its high flexibility around the immunoglobulin-like domain which may act also as a pivot. These results represent new structural and functional information useful on biotechnological applications for biofuel and food industries. (AU)

FAPESP's process: 13/26096-4 - Heterologous expression of the chitinase enzyme of Leishmania (L.) infantum chagasi, Leishmania (V.) braziliensis and Leishmania (V.) amazonensis: serological diagnosis and comparative molecular study using expression systems of insects cell and bacteria
Grantee:Aline Diniz Cabral
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 16/15836-5 - Modular Hyperthermostable endo-beta-1,4-mannanase: determination of the three-dimensional structure of the central domain and its role in the thermostabilization of whole enzyme
Grantee:Viviam Moura da Silva
Support type: Scholarships abroad - Research Internship - Doctorate
FAPESP's process: 17/17275-3 - Studies of the mode of action of two Lytic Polysaccharide Monooxygenases from insect (order: Isoptera): molecular structure, bioinorganic chemistry and biotechnological applications
Grantee:Wanius José Garcia da Silva
Support type: Regular Research Grants
FAPESP's process: 17/16291-5 - Structural and biophysical characterization of thermophilic enzymes prospected from the fungus Thielavia terrestris for biomass degradation and biotechnological products generation
Grantee:João Renato Carvalho Muniz
Support type: Regular Research Grants
FAPESP's process: 14/02065-5 - Modular Hyperthermostable endo-beta-1,4-mannanase: determination of the three-dimensional structure of the Central Domain an its role in the thermostabilization of whole enzyme
Grantee:Viviam Moura da Silva
Support type: Scholarships in Brazil - Doctorate
FAPESP's process: 16/14514-4 - Characterization of the chitinase from South American endemic Leishmania species: use in diagnosis in humans, dogs and sandflies
Grantee:Marcia Aparecida Speranca
Support type: Regular Research Grants
FAPESP's process: 14/50897-0 - Open-acess Medicinal Chemistry Centre (OpenMedChem)
Grantee:Paulo Arruda
Support type: Research Projects - Thematic Grants
FAPESP's process: 15/50590-4 - Lignin valorization in cellulosic ethanol plants: biocatalytic conversion via feluric acid to high value chemicals
Grantee:Fábio Márcio Squina
Support type: Program for Research on Bioenergy (BIOEN) - Thematic Grants