3vgi

Publication Abstract from PubMed

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 (EGPfDeltaN30) 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 A. 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 Ca(2)(+) in a DxDxDG Ca(2)(+)-binding motif, atypical of most archaeal proteins.

Atomic resolution of the crystal structure of the hyperthermophilic family 12 endocellulase and stabilizing role of the DxDxDG calcium-binding motif in Pyrococcus furiosus.,Kim HW, Kataoka M, Ishikawa K FEBS Lett. 2012 Apr 5;586(7):1009-13. Epub 2012 Mar 6. PMID:22569255^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.