2CL2

Endo-1,3(4)-beta-glucanase from Phanerochaete chrysosporium, solved using native sulfur SAD, exhibiting intact heptasaccharide glycosylation

Summary for 2CL2

• Entry DOI: 10.2210/pdb2cl2/pdb
• Descriptor: PUTATIVE LAMINARINASE, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: glycosyl hydrolase, gh16, family 16, laminarinase, laminarin, beta-glucanase, basidiomycete, white rot fungus, gh7, beta-1, 3/1, 6-glucan, lam16a, pichea pastoris, extracellular, beta sandwich, hydrolase
• Biological source: PHANEROCHAETE CHRYSOSPORIUM (WHITE-ROT FUNGUS)
• Total number of polymer chains: 1
• Total formula weight: 33157.83

Authors

Vasur, J.,Kawai, R.,Igarashi, K.,Sandgren, M.,Samejima, M.,Stahlberg, J. (deposition date: 2006-04-25, release date: 2006-10-25, Last modification date: 2024-10-16)

Primary citation

Vasur, J.,Kawai, R.,Larsson, A.M.,Igarashi, K.,Sandgren, M.,Samejima, M.,Stahlberg, J.
X-ray crystallographic native sulfur SAD structure determination of laminarinase Lam16A from Phanerochaete chrysosporium.
Acta Crystallogr. D Biol. Crystallogr., 62:1422-1429, 2006

PubMed Abstract: 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.

PubMed: 17057348
DOI: 10.1107/S0907444906036407

Experimental method

X-RAY DIFFRACTION (1.35 Å)