Atomic resolution of the crystal structure of the hyperthermophilic family 12 endocellulase and stabilizing role of the DxDxDG calcium-binding motif in Pyrococcus furiosus

[摘要]：Hyperthermophilic glycoside hydrolase family 12 endocellulase (EGPf) from the archaeon Pyrococcus furiosus catalyzes the hydrolytic cleavage of beta-1,4-glucosidic linkage in beta-glucan cellulose. A truncated EGPf (EGPf Delta N30) mutant lacking the proline and hydroxyl-residue rich region at the N terminus was constructed, and its crystal structure was resolved at an atomic resolution of 1.07 angstrom. Our results indicate that the structure of EGPf, which consists of a beta-jelly roll, exhibits structural similarity with the endocellulase of Thermotoga maritima. Additionally, we further determined that the thermostability of EGPf is maintained in part by the binding of Ca2+ in a DxDxDG Ca2+-binding motif, atypical of most archaeal proteins. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

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