Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/89651
Type: Artigo de periódico
Title: Small-angle X-ray Scattering And Structural Modeling Of Full-length: Cellobiohydrolase I From Trichoderma Harzianum
Author: Lima L.H.F.
Serpa V.I.
Rosseto F.R.
Sartori G.R.
de Oliveira Neto M.
Martinez L.
Polikarpov I.
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.
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Rights: fechado
Identifier DOI: 10.1007/s10570-013-9933-3
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-84881023746&partnerID=40&md5=6eb4bbef88e26c681ae1d6dd0d462f36
Date Issue: 2013
Appears in Collections:Unicamp - Artigos e Outros Documentos

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