2vy0 | pdb_00002vy0

THE X-RAY STRUCTURE OF ENDO-BETA-1,3-GLUCANASE FROM PYROCOCCUS FURIOSUS

spinqualitylabelsall models 2vy0, resolution 2.16Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vy0 is a 2 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, CL, MPD, MRD, NA Activity: Glucan endo-1,3-beta-D-glucosidase, with EC number 3.2.1.39 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Bacterial and archaeal endo-beta-1,3-glucanases that belong to glycoside hydrolase family 16 share a beta-jelly-roll fold, but differ significantly in sequence and in substrate specificity. The crystal structure of the laminarinase (EC 3.2.1.39) from the hyperthermophilic archaeon Pyrococcus furiosus (pfLamA) has been determined at 2.1 A resolution by molecular replacement. The pfLamA structure reveals a kink of six residues (72-77) at the entrance of the catalytic cleft. This peptide is absent in the endoglucanases from alkaliphilic Nocardiopsis sp. strain F96 and Bacillus macerans, two proteins displaying an overall fold similar to that of pfLamA, but with different substrate specificity. A deletion mutant of pfLamA, lacking residues 72-75, hydrolyses the mixed-linkage beta-1,3-1,4-glucan lichenan 10 times more efficiently than the wild-type protein, indicating the importance of the kink in substrate preference. Crystal structure of a family 16 endoglucanase from the hyperthermophile Pyrococcus furiosus--structural basis of substrate recognition.,Ilari A, Fiorillo A, Angelaccio S, Florio R, Chiaraluce R, van der Oost J, Consalvi V FEBS J. 2009 Feb;276(4):1048-58. Epub 2008 Jan 16. PMID:19154353 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glucanase

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