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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/76109
Title: 
Small-angle X-ray scattering and structural modeling of full-length: Cellobiohydrolase I from Trichoderma harzianum
Author(s): 
Institution: 
  • Universidade de São Paulo (USP)
  • Universidade Estadual Paulista (UNESP)
  • Universidade Estadual de Campinas (UNICAMP)
ISSN: 
0969-0239
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. © 2013 Springer Science+Business Media Dordrecht.
Issue Date: 
1-Aug-2013
Citation: 
Cellulose, v. 20, n. 4, p. 1573-1585, 2013.
Time Duration: 
1573-1585
Keywords: 
  • CBH1
  • Cellobiohydrolase
  • Cellulose
  • Trichoderma
  • Biotechnological applications
  • Cellobiohydrolases
  • Cellulose-binding domain
  • Intramolecular interactions
  • Small angle X-ray scattering
  • Two-domain architecture
  • Cellulosic ethanol
  • Molecular structure
  • Peptides
  • X ray scattering
Source: 
http://dx.doi.org/10.1007/s10570-013-9933-3
URI: 
Access Rights: 
Acesso restrito
Type: 
outro
Source:
http://repositorio.unesp.br/handle/11449/76109
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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