2wne

MUTANT LAMINARINASE 16A CYCLIZES LAMINARIHEPTAOSE

spinqualitylabelsall models 2wne, resolution 2.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wne is a 1 chain structure with sequence from Phanerochaete chrysosporium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BGC, BMA, GLC, MAN, NAG Related: 2wlq, 2w39, 2w52, 2cl2 Activity: Endo-1,3(4)-beta-glucanase, with EC number 3.2.1.6 Resources: FirstGlance, OCA, 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 Glycosynthases are precise molecular instruments for making specifically linked oligosaccharides. X-ray crystallography screening of ligands bound to the 1,3(4)-beta-d-glucanase nucleophile mutant E115S of Phanerochaete chrysosporium Laminarinase 16A (Lam16A) showed that laminariheptaose (L7) bound in an arch with the reducing and nonreducing ends occupying either side of the catalytic cleft of the enzyme. The X-ray structure of Lam16A E115S in complex with alpha-laminariheptaosyl fluoride (alphaL7F) revealed how alphaL7F could make a nucleophilic attack upon itself. Indeed, when Lam16A E115S was allowed to react with alphaL7F the major product was a cyclic beta-1,3-heptaglucan, as shown by mass spectrometry. NMR confirmed uniquely beta-1,3-linkages and no reducing end. Molecular dynamics simulations indicate that the cyclic laminariheptaose molecule is not completely planar and that torsion angles at the glycosidic linkages fluctuate between two energy minima. This is the first report of a glycosynthase that joins the reducing and nonreducing ends of a single oligosaccharide and the first reported synthesis of cyclic beta-glucan. Synthesis of Cyclic beta-Glucan Using Laminarinase 16A Glycosynthase Mutant from the Basidiomycete Phanerochaete chrysosporium.,Vasur J, Kawai R, Jonsson KH, Widmalm G, Engstrom A, Frank M, Andersson E, Hansson H, Forsberg Z, Igarashi K, Samejima M, Sandgren M, Stahlberg J J Am Chem Soc. 2010 Jan 15. PMID:20078120 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA