2wq8 | pdb_00002wq8

Glycan labelling using engineered variants of galactose oxidase obtained by directed evolution

spinqualitylabelsall models 2wq8, resolution 2.19Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wq8 is a 1 chain structure with sequence from Fusairum graminearum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACY, CA, CU, EDO, GOL Related: 2jkx, 2vz3, 1gof, 1k3i, 1t2x, 1goh, 2vz1, 1gog Activity: Galactose oxidase, with EC number 1.1.3.9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GAOA_GIBZE] Catalyzes the sterospecific oxidation of primary alcohols to the corresponding aldehydes. The biologically relevant substrate of the enzyme is not known as the enzyme exhibits broad substrate specificity from small alcohols through sugars to oligo- and polysaccharides (By similarity). 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 A directed evolution approach has been used for the generation of variants of galactose oxidase (GOase) that can selectively oxidize glycans on glycoproteins. The aldehyde function introduced on the glycans d-mannose (Man) and d-N-acetyl glucosamine (GlcNAc) by the enzyme variants could then be used to label the glycoproteins and also whole cells that display mannosides on their surface. Glycoprotein labeling using engineered variants of galactose oxidase obtained by directed evolution.,Rannes JB, Ioannou A, Willies SC, Grogan G, Behrens C, Flitsch SL, Turner NJ J Am Chem Soc. 2011 Jun 8;133(22):8436-9. Epub 2011 May 12. PMID:21526835 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Galactose oxidase

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