Journal
JOURNAL OF STRUCTURAL BIOLOGY
Volume 177, Issue 2, Pages 469-476Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2011.11.021
Keywords
Mannan endo-1,4-beta-mannosidase; Glycoside hydrolase family 5; Carbohydrate binding module 27; Thermotoga petrophila RKU-1; Crystal structure; Substrate recognition
Funding
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo [10/51890-8]
- Department of Energy [06103-OKL, ZDJ-7-77608-01]
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [10/51890-8] Funding Source: FAPESP
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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.
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