Lima, Leonardo H.F.Serpa, Viviane I.Rosseto, Flávio R.Sartori, Geraldo Rodriguesde Oliveira Neto, Mario [UNESP]Martínez, LeandroPolikarpov, Igor2014-05-272014-05-272013-08-01Cellulose, v. 20, n. 4, p. 1573-1585, 2013.0969-0239http://hdl.handle.net/11449/76109Cellobiohydrolases 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.1573-1585engCBH1CellobiohydrolaseCelluloseTrichodermaBiotechnological applicationsCellobiohydrolasesCellulose-binding domainIntramolecular interactionsSmall angle X-ray scatteringTwo-domain architectureCellulosic ethanolMolecular structurePeptidesX ray scatteringArtigo10.1007/s10570-013-9933-3Acesso restrito2-s2.0-848810237468213371495151651