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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

Grant number: 16/15836-5
Support type:Scholarships abroad - Research Internship - Doctorate
Effective date (Start): January 16, 2017
Effective date (End): January 15, 2018
Field of knowledge:Biological Sciences - Biophysics - Molecular Biophysics
Principal researcher:Wanius José Garcia da Silva
Grantee:Viviam Moura da Silva
Supervisor abroad: Yvain Nicolet
Home Institution: Centro de Ciências Naturais e Humanas (CCNH). Universidade Federal do ABC (UFABC). Ministério da Educação (Brasil). Santo André , SP, Brazil
Research place: Institut de Biologie Structurale (IBS), France  
Associated to the scholarship: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, BP.DR

Abstract

The complete enzymatic hydrolysis of mannan polysaccharides requires at least three types of enzymes working synergistically: ²-mannanase, ²-mannosidase, and ²-glucosidase. The hyperthermophilic bacterium Thermotoga petrophila produces the enzyme endo-²-1,4-mannanse (TpMan), which is composed of a GH5 catalytic domain and a carbohydrate-binding domain connected through a linker. The crystal structure of the GH5 catalytic domain was determined, however, to date, there is no three-dimensional structure available for the full-length TpMan. Recently, we reported the first low-resolution model for the full-length TpMan and demonstrated that the linker is a compact domain. In this scientific project, as part of a continuing investigation of TpMan, we propose to determine the three-dimensional structure of the full-length enzyme (TpMan) and/or of its central domain (linker) using X-ray crystallography. Our previous attempts to crystallize the full-length TpMan and the linker were so far unsuccessful. Therefore, an internship in a center such as the Institut de Biologie Structurale - Grenoble/France with extensive experience in X-ray crystallography, should certainly be essential in determining the TpMan structure.

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Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
DA SILVA, VIVIAM M.; CABRAL, ALINE D.; SPERANCA, MARCIA A.; SQUINA, FABIO M.; MUNIZ, JOAO RENATO C.; MARTIN, LYDIE; NICOLET, YVAIN; GARCIA, WANIUS. High-resolution structure of a modular hyperthermostable endo-beta-1,4-mannanase from Thermotoga petrophila: The ancillary immunoglobulin-like module is a thermostabilizing domain. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, v. 1868, n. 8, . (13/26096-4, 16/15836-5, 17/17275-3, 17/16291-5, 14/02065-5, 16/14514-4, 14/50897-0, 15/50590-4)

Please report errors in scientific publications list by writing to: cdi@fapesp.br.