2cl2

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Template:STRUCTURE 2cl2

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

Overview

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.

About this Structure

2CL2 is a Single protein structure of sequence from Phanerochaete chrysosporium. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 22:23:47 2008