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 Pseudo-alteromonas 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

Published in

Acta Crystallographica Section D: Biological Crystallography
2006, Volume: 62, pages: 1422-1429
Publisher: BLACKWELL PUBLISHING

SLU Authors

• Vasur, Jonas

  • Department of Molecular Biology, Swedish University of Agricultural Sciences
    

• Sandgren, Mats

  • Department of Molecular Biology, Swedish University of Agricultural Sciences
    

• Ståhlberg, Jerry

  • Department of Molecular Biology, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Agricultural Science
Forest Science
Renewable Bioenergy Research


Publication identifier

DOI: https://doi.org/10.1107/S0907444906036407

Permanent link to this page (URI)

https://res.slu.se/id/publ/9900