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Joint X ‐ray crystallographic and molecular dynamics study of cellobiohydrolase I from T richoderma harzianum : deciphering the structural features of cellobiohydrolase catalytic activity
Author(s) -
Textor Larissa C.,
Colussi Francieli,
Silveira Rodrigo L.,
Serpa Viviane,
Mello Bruno L.,
Muniz João Renato C.,
Squina Fabio M.,
Pereira Nei,
Skaf Munir S.,
Polikarpov Igor
Publication year - 2013
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12049
Subject(s) - trichoderma reesei , trichoderma harzianum , chemistry , cellulase , molecular dynamics , substrate (aquarium) , crystallography , stereochemistry , cellulose , biochemistry , biology , computational chemistry , botany , ecology , biological pest control
Aiming to contribute toward the characterization of new, biotechnologically relevant cellulolytic enzymes, we report here the first crystal structure of the catalytic core domain of C el7A (cellobiohydrolase I) from the filamentous fungus T richoderma harzianum IOC 3844. Our structural studies and molecular dynamics simulations show that the flexibility of T yr260, in comparison with T yr247 from the homologous T richoderma reesei C el7A, is enhanced as a result of the short side‐chains of adjacent V al216 and A la384 residues and creates an additional gap at the side face of the catalytic tunnel. T . harzianum cellobiohydrolase I also has a shortened loop at the entrance of the cellulose‐binding tunnel, which has been described to interact with the substrate in T . reesei C el7 A . These structural features might explain why T . harzianum C el7 A displays higher k cat and K m values, and lower product inhibition on both glucoside and lactoside substrates, compared with T . reesei C el7 A .