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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Molecular insights into substrate specificity and thermal stability of a bacterial GH5-CBM27 endo-1,4-beta-D-mannanase

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Author(s):
dos Santos, Camila Ramos [1] ; Paiva, Joice Helena [1] ; Meza, Andreia Navarro [1] ; Cota, Junio [2] ; Alvarez, Thabata Maria [2] ; Ruller, Roberto [2] ; Prade, Rolf Alexander [3] ; Squina, Fabio Marcio [2] ; Murakami, Mario Tyago [1]
Total Authors: 9
Affiliation:
[1] Ctr Nacl Pesquisa Energia & Mat, Lab Nacl Biociencias LNBio, BR-13083970 Campinas, SP - Brazil
[2] Ctr Nacl Pesquisa Energia & Mat, Lab Nacl Ciencia & Tecnol Bioetanol CTBE, BR-13083970 Campinas, SP - Brazil
[3] Oklahoma State Univ, Dept Microbiol & Mol Genet, Stillwater, OK 74078 - USA
Total Affiliations: 3
Document type: Journal article
Source: Journal of Structural Biology; v. 177, n. 2, p. 469-476, FEB 2012.
Web of Science Citations: 18
Abstract

The breakdown of beta-1,4-mannoside linkages in a variety of mannan-containing polysaccharides is of great importance in industrial processes such as kraft pulp delignification, food processing and production of second-generation biofuels, which puts a premium on studies regarding the prospection and engineering of beta-mannanases. In this work, a two-domain beta-mannanase from Thermotoga petrophila that encompasses a GH5 catalytic domain with a C-terminal CBM27 accessory domain, was functionally and structurally characterized. Kinetic and thermal denaturation experiments showed that the CBM27 domain provided thermo-protection to the catalytic domain, while no contribution on enzymatic activity was observed. The structure of the catalytic domain determined by SIRAS revealed a canonical (alpha/beta)(8)-barrel scaffold surrounded by loops and short helices that form the catalytic interface. Several structurally related ligand molecules interacting with TpMan were solved at high-resolution and resulted in a wide-range representation of the subsites forming the active-site cleft with residues W134, E198, R200, E235, H283 and W284 directly involved in glucose binding. (C) 2011 Elsevier Inc. All rights reserved. (AU)

FAPESP's process: 10/51890-8 - SMOLBnet 2.0: Structural studies of transcription factors involved in the regulation of hydrolytic enzyme genes and swollenin from Aspergillus niger and A. fumigatus
Grantee:Mário Tyago Murakami
Support Opportunities: Regular Research Grants