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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.)

Small-angle X-ray scattering and structural modeling of full-length: cellobiohydrolase I from Trichoderma harzianum

Full text
Author(s):
Lima, Leonardo H. F. [1] ; Serpa, Viviane I. [1] ; Rosseto, Flavio R. [1] ; Sartori, Geraldo Rodrigues [1] ; de Oliveira Neto, Mario [1] ; Martinez, Leandro [1] ; Polikarpov, Igor [1]
Total Authors: 7
Affiliation:
[1] Univ Sao Paulo, Grp Biotecnol Mol, IFSC, BR-13566570 Sao Carlos, SP - Brazil
Total Affiliations: 1
Document type: Journal article
Source: Cellulose; v. 20, n. 4, p. 1573-1585, AUG 2013.
Web of Science Citations: 7
Abstract

Cellobiohydrolases hydrolyze cellulose releasing cellobiose units. They are very important for a number of biotechnological applications, such as, for example, production of cellulosic ethanol and cotton fiber processing. The Trichoderma cellobiohydrolase I (CBH1 or Cel7A) is an industrially important exocellulase. It exhibits a typical two domain architecture, with a small C-terminal cellulose-binding domain and a large N-terminal catalytic core domain, connected by an O-glycosylated linker peptide. The mechanism by which the linker mediates the concerted action of the two domains remains a conundrum. Here, we probe the protein shape and domain organization of the CBH1 of Trichoderma harzianum (ThCel7A) by small angle X-ray scattering (SAXS) and structural modeling. Our SAXS data shows that ThCel7A linker is partially-extended in solution. Structural modeling suggests that this linker conformation is stabilized by inter- and intra-molecular interactions involving the linker peptide and its O-glycosylations. (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: 07/08706-9 - Molecular and Structural Studies of Cellulitic Complex Enzymes of Fungi Trichoderma harzianum with Potencial of Enzymatic Transformation of Biomass
Grantee:Viviane Isabel Serpa
Support Opportunities: Scholarships in Brazil - 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 Opportunities: Program for Research on Bioenergy (BIOEN) - Thematic Grants
FAPESP's process: 08/05637-9 - Structural studies of the three isotypes of the peroxisomal proliferator-activated receptor hPPAR and them interaction with retinoid receptor hRXRalfa using small angle X-ray scattering
Grantee:Mario de Oliveira Neto
Support Opportunities: Scholarships in Brazil - Post-Doctoral
FAPESP's process: 10/16947-9 - Correlations between dynamics, structure and function in protein: computer simulations and algorithms
Grantee:Leandro Martinez
Support Opportunities: Regular Research Grants