Advanced search
Start date
Betweenand
Related content
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Joint X-ray crystallographic and molecular dynamics study of cellobiohydrolase I from Trichoderma harzianum: deciphering the structural features of cellobiohydrolase catalytic activity

Full text
Author(s):
Textor, Larissa C. [1] ; Colussi, Francieli [1] ; Silveira, Rodrigo L. [2] ; Serpa, Viviane [1] ; de Mello, Bruno L. [1] ; Muniz, Joao Renato C. [1] ; Squina, Fabio M. [3] ; Pereira, Jr., Nei [4] ; Skaf, Munir S. [2] ; Polikarpov, Igor [1]
Total Authors: 10
Affiliation:
[1] Univ Sao Paulo, Inst Fis Sao Carlos, BR-13560970 Sao Carlos, SP - Brazil
[2] State Univ Campinas UNICAMP, Inst Chem, Campinas, SP - Brazil
[3] CNPEM, Lab Nacl Ciencia & Tecnol Bioetanol CTBE, Campinas, SP - Brazil
[4] Univ Fed Rio de Janeiro, Escola Quim, Ctr Tecnol, Lab Desenvolvimento Bioproc LaDeBio, BR-21941 Rio De Janeiro - Brazil
Total Affiliations: 4
Document type: Journal article
Source: FEBS Journal; v. 280, n. 1, p. 56-69, JAN 2013.
Web of Science Citations: 32
Abstract

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 Cel7A (cellobiohydrolase I) from the filamentous fungus Trichoderma harzianum IOC 3844. Our structural studies and molecular dynamics simulations show that the flexibility of Tyr260, in comparison with Tyr247 from the homologous Trichoderma reesei Cel7A, is enhanced as a result of the short side-chains of adjacent Val216 and Ala384 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 Cel7A. These structural features might explain why T. harzianum Cel7A displays higher kcat and Km values, and lower product inhibition on both glucoside and lactoside substrates, compared with T. reesei Cel7A. (AU)

FAPESP's process: 09/54035-4 - Facility for advanced studies of biosystems and nanostructured materials
Grantee:Igor Polikarpov
Support Opportunities: Multi-user Equipment Program
FAPESP's process: 10/08680-2 - Molecular aspectos of lignocellulosic biomass degradation: dynamics of enzymes and plant cell wall nanoarchitecture
Grantee:Rodrigo Leandro Silveira
Support Opportunities: Scholarships in Brazil - Doctorate