3vgi | pdb_00003vgi

The crystal structure of hyperthermophilic family 12 endocellulase from Pyrococcus furiosus

spinqualitylabelsall models 3vgi, resolution 1.07Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vgi is a 1 chain structure with sequence from Atcc 43587. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, GOL, NHE Related: 3az0 Gene: eglA (ATCC 43587) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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