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

FEBS Letters
Han-Woo KimKazuhiko Ishikawa

Abstract

Hyperthermophilic glycoside hydrolase family 12 endocellulase (EGPf) from the archaeon Pyrococcus furiosus catalyzes the hydrolytic cleavage of β-1,4-glucosidic linkage in β-glucan cellulose. A truncated EGPf (EGPfΔN30) 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 Å. Our results indicate that the structure of EGPf, which consists of a β-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.

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Citations

Oct 28, 2015·International Journal of Molecular Sciences·Junling WangZuoming Zhang
Apr 30, 2014·Advances in Bioinformatics·Tatyana Aleksandrovna Khrustaleva
Nov 13, 2014·Journal of Industrial Microbiology & Biotechnology·Seiichiro KishishitaKazuhiko Ishikawa
Sep 12, 2014·Bioscience, Biotechnology, and Biochemistry·Misumi Kataoka, Kazuhiko Ishikawa
Jul 10, 2014·Acta Crystallographica. Section F, Structural Biology Communications·Misumi Kataoka, Kazuhiko Ishikawa
Jan 30, 2015·Chemical Reviews·Christina M PayneGregg T Beckham

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