PDBsum entry 3vgi

Hydrolase

PDB id: 3vgi

Contents

Protein chain

270 a.a.

Ligands

NHE ×2

GOL ×11

Metals

_CA

Waters ×328

References listed in PDB file

Key reference

• Title: Atomic resolution of the crystal structure of the hyperthermophilic family 12 endocellulase and stabilizing role of the dxdxdg calcium-Binding motif in pyrococcus furiosus.
• Authors: H.W.Kim, M.Kataoka, K.Ishikawa.
• Ref.: Febs Lett, 2012, 586, 1009-1013.
• PubMed id: 22569255

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.