4bq1

Crystal structure of of LamAcat from Zobellia galactanivorans

spinqualitylabelsall models 4bq1, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bq1 is a 2 chain structure with sequence from "cytophaga_drobachiensis"_barbeyron_et_al._1998 "cytophaga drobachiensis" barbeyron et al. 1998. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, GOL Related: 4bow, 4bpz Activity: Glucan endo-1,3-beta-D-glucosidase, with EC number 3.2.1.39 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Laminarinase is commonly used to describe [beta]-1,3-glucanases widespread throughout Archaea, bacteria and several eukaryotic lineages. Some [beta]-1,3-glucanases have already been structurally and biochemically characterized, but very few from organisms that are in contact with genuine laminarin, the storage polysaccharide of brown algae. Here we report the heterologous expression and subsequent biochemical and structural characterization of ZgLamAGH16 from Zobellia galactanivorans, the first GH16 laminarinase from a marine bacterium associated with seaweeds. ZgLamAGH16 contains a unique additional loop, compared to other GH16 laminarinases, which is composed of 17 amino-acids and gives a bent shape to the active cleft of the enzyme. This particular topology is perfectly adapted to the U-shape conformation of laminarin chains in solution, and thus explains the predominant specificity of ZgLamAGH16 for this substrate. The 3D structure of the enzyme and two enzyme-substrate complexes, one with laminaritetraose, the other with a trisaccharide of 1,3-1,4-[beta]-D-glucan, have been determined at 1.5 A, 1.35 A and 1.13 A resolution, respectively. The structural comparison of substrate recognition pattern between these complexes allow the proposition that ZgLamAGH16 likely diverged from an ancestral broad specificity GH16 beta-glucanase and evolved toward a bent active site topology adapted to efficient degradation of algal laminarin. The beta-Glucanase ZgLamA from Zobellia galactanivorans evolved a bent active site adapted for efficient degradation of algal laminarin.,Labourel A, Jam M, Jeudy A, Hehemann JH, Czjzek M, Michel G J Biol Chem. 2013 Dec 11. PMID:24337571 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glucanase

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