dc.contributor | Universidade de São Paulo (USP) | |
dc.contributor | Universidade Estadual Paulista (Unesp) | |
dc.contributor | Universidade Estadual de Campinas (UNICAMP) | |
dc.date.accessioned | 2014-05-27T11:30:04Z | |
dc.date.accessioned | 2022-10-05T18:55:57Z | |
dc.date.available | 2014-05-27T11:30:04Z | |
dc.date.available | 2022-10-05T18:55:57Z | |
dc.date.created | 2014-05-27T11:30:04Z | |
dc.date.issued | 2013-08-01 | |
dc.identifier | Cellulose, v. 20, n. 4, p. 1573-1585, 2013. | |
dc.identifier | 0969-0239 | |
dc.identifier | http://hdl.handle.net/11449/76109 | |
dc.identifier | 10.1007/s10570-013-9933-3 | |
dc.identifier | 2-s2.0-84881023746 | |
dc.identifier | 8213371495151651 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/3925010 | |
dc.description.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. | |
dc.language | eng | |
dc.relation | Cellulose | |
dc.relation | 3.809 | |
dc.relation | 1,047 | |
dc.rights | Acesso restrito | |
dc.source | Scopus | |
dc.subject | CBH1 | |
dc.subject | Cellobiohydrolase | |
dc.subject | Cellulose | |
dc.subject | Trichoderma | |
dc.subject | Biotechnological applications | |
dc.subject | Cellobiohydrolases | |
dc.subject | Cellulose-binding domain | |
dc.subject | Intramolecular interactions | |
dc.subject | Small angle X-ray scattering | |
dc.subject | Two-domain architecture | |
dc.subject | Cellulosic ethanol | |
dc.subject | Molecular structure | |
dc.subject | Peptides | |
dc.subject | X ray scattering | |
dc.title | Small-angle X-ray scattering and structural modeling of full-length: Cellobiohydrolase I from Trichoderma harzianum | |
dc.type | Artigo | |