2atm | pdb_00002atm

Crystal structure of the recombinant allergen Ves v 2

spinqualitylabelsall models 2atm, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2atm is a 1 chain structure with sequence from Paravespula vulgaris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MES, SO4 NonStd Res: SME Activity: Hydrolase, with EC number 3.2.1.35 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [HUGAA_VESVU] Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides. 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 Wasp venom from Vespula vulgaris contains three major allergens: Ves v 1, Ves v 2 and Ves v 5. Here, the cloning, expression, biochemical characterization and crystal structure determination of the hyaluronidase Ves v 2 from family 56 of the glycoside hydrolases are reported. The allergen was expressed in Escherichia coli as an insoluble protein and refolded and purified to obtain full enzymatic activity. Three N-glycosylation sites at Asn79, Asn99 and Asn127 were identified in Ves v 2 from a natural source by enzymatic digestions combined with MALDI-TOF mass spectrometry. The crystal structure of recombinant Ves v 2 was determined at 2.0 A resolution and reveals a central (beta/alpha)(7) core that is further stabilized by two disulfide bonds (Cys19-Cys308 and Cys185-Cys197). Based on sequence alignments and structural comparison with the honeybee allergen Api m 2, it is proposed that a conserved cavity near the active site is involved in binding of the substrate. Surface epitopes and putative glycosylation sites have been compared with those of two other major group 2 allergens from Apis mellifera (honeybee) and Dolichovespula maculata (white-faced hornet). The analysis suggests that the harboured allergic IgE-mediated cross-reactivity between Ves v 2 and the allergen from D. maculata is much higher than that between Ves v 2 and the allergen from A. mellifera. Structure of recombinant Ves v 2 at 2.0 Angstrom resolution: structural analysis of an allergenic hyaluronidase from wasp venom.,Skov LK, Seppala U, Coen JJ, Crickmore N, King TP, Monsalve R, Kastrup JS, Spangfort MD, Gajhede M Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):595-604. Epub 2006, May 12. PMID:16699186 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hyaluronidase 3D structures

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