2cl2 | pdb_00002cl2

ENDO-1,3(4)-BETA-GLUCANASE FROM PHANEROCHAETE CHRYSOSPORIUM, SOLVED USING NATIVE SULFUR SAD, EXHIBITING INTACT HEPTASACCHARIDE GLYCOSYLATION

spinqualitylabelsall models 2cl2, resolution 1.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2cl2 is a 1 chain structure with sequence from Chrysosporium pruinosum (gilman & abbott) carmich.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, MAN, NAG Activity: Endo-1,3(4)-beta-glucanase, with EC number 3.2.1.6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum 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 Laminarinase Lam16A from Phanerochaete chrysosporium was recombinantly expressed in Pichia pastoris, crystallized and the structure was solved at 1.34 A resolution using native sulfur SAD X-ray crystallography. It is the first structure of a non-specific 1,3(4)-beta-D-glucanase from glycoside hydrolase family 16 (GH16). P. chrysosporium is a wood-degrading basidiomycete fungus and Lam16A is the predominant extracellular protein expressed when laminarin is used as the sole carbon source. The protein folds into a curved beta-sandwich homologous to those of other known GH16 enzyme structures (especially kappa-carrageenase from Pseudoalteromonas carrageenovora and beta-agarase from Zobelia galactanivorans). A notable likeness is also evident with the related glycoside hydrolase family 7 (GH7) enzymes. A mammalian lectin, p58/ERGIC, as well as polysaccharide lyase (PL7) enzymes also showed significant similarity to Lam16A. The enzyme has two potential N-glycosylation sites. One such site, at Asn43, displayed a branched heptasaccharide sufficiently stabilized to be interpreted from the X-ray diffraction data. The other N-glycosylation motif was found close to the catalytic centre and is evidently not glycosylated. X-ray crystallographic native sulfur SAD structure determination of laminarinase Lam16A from Phanerochaete chrysosporium.,Vasur J, Kawai R, Larsson AM, Igarashi K, Sandgren M, Samejima M, Stahlberg J Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1422-9. Epub 2006, Oct 18. PMID:17057348 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glucanase

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