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3VGI

The crystal structure of hyperthermophilic family 12 endocellulase from Pyrococcus furiosus

Summary for 3VGI
Entry DOI10.2210/pdb3vgi/pdb
Related3AZ0
DescriptorEndoglucanase A, CALCIUM ION, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID, ... (5 entities in total)
Functional Keywordsbeta-jelly roll fold, hydrolase, carbohydrate/sugar binding
Biological sourcePyrococcus furiosus
Total number of polymer chains1
Total formula weight37483.27
Authors
Kataoka, M.,Kim, H.-W.,Ishikawa, K. (deposition date: 2011-08-11, release date: 2012-09-12, Last modification date: 2024-03-20)
Primary citationKim, H.-W.,Kataoka, M.,Ishikawa, K.
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, 2012
Cited by
PubMed 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.
PubMed: 22569255
DOI: 10.1016/j.febslet.2012.02.029
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.07 Å)
Structure validation

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数据于2025-08-06公开中

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