2ATM

Crystal structure of the recombinant allergen Ves v 2

Summary for 2ATM

• Entry DOI: 10.2210/pdb2atm/pdb
• Descriptor: Hyaluronoglucosaminidase, SULFATE ION, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: beta-alpha-barrels, hydrolase
• Biological source: Vespula vulgaris
• Cellular location: Secreted: P49370
• Total number of polymer chains: 1
• Total formula weight: 39291.62

Authors

Skov, L.K.,Seppala, U.,Coen, J.J.F.,Crickmore, N.,King, T.P.,Monsalve, R.,Kastrup, J.S.,Spangfort, M.D.,Gajhede, M. (deposition date: 2005-08-25, release date: 2006-05-23, Last modification date: 2023-10-25)

Primary citation

Skov, L.K.,Seppala, U.,Coen, J.J.,Crickmore, N.,King, T.P.,Monsalve, R.,Kastrup, J.S.,Spangfort, M.D.,Gajhede, M.
Structure of recombinant Ves v 2 at 2.0 Angstrom resolution: structural analysis of an allergenic hyaluronidase from wasp venom.
Acta Crystallogr.,Sect.D, 62:595-604, 2006

PubMed Abstract: 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.

PubMed: 16699186
DOI: 10.1107/S0907444906010687

Experimental method

X-RAY DIFFRACTION (2 Å)