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

Kim Han-Woo | Zendy; Kataoka Misumi | Zendy; Ishikawa Kazuhiko | Zendy

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

Author(s) -

Kim Han-Woo,

Kataoka Misumi,

Ishikawa Kazuhiko

Publication year - 2012

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2012.02.029

Subject(s) - pyrococcus furiosus , thermotoga maritima , thermostability , hyperthermophile , glycoside hydrolase , chemistry , hydrolase , thermophile , crystallography , biochemistry , pyrococcus horikoshii , lyase , stereochemistry , hydrolysis , archaea , crystal structure , enzyme , gene , escherichia coli

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 ofCa 2 +in a DxDxDGCa 2 +‐binding motif, atypical of most archaeal proteins.

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