H.W.Kim
et al.
(2012).
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 Lett,
586,
1009-1013.
PubMed id: 22569255
Atomic resolution of the crystal structure of the hyperthermophilic family 12 endocellulase and stabilizing role of the DxDxDG calcium-binding motif in Pyrococcus furiosus.
H.W.Kim,
M.Kataoka,
K.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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