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- Title
Small-angle X-ray scattering and structural modeling of full-length: cellobiohydrolase I from Trichoderma harzianum.
- Authors
Lima, Leonardo; Serpa, Viviane; Rosseto, Flávio; Sartori, Geraldo; Oliveira Neto, Mario; Martínez, Leandro; Polikarpov, Igor
- 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.
- Subjects
TRICHODERMA harzianum; X-ray scattering; CELLULOSE 1,4-beta-cellobiosidase; HYDROLYSIS; DEHYDRATION reactions
- Publication
Cellulose, 2013, Vol 20, Issue 4, p1573
- ISSN
0969-0239
- Publication type
Article
- DOI
10.1007/s10570-013-9933-3