2atm
From Proteopedia
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|PDB= 2atm |SIZE=350|CAPTION= <scene name='initialview01'>2atm</scene>, resolution 2.000Å | |PDB= 2atm |SIZE=350|CAPTION= <scene name='initialview01'>2atm</scene>, resolution 2.000Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SME:METHIONINE+SULFOXIDE'>SME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
- | |ACTIVITY= [http://en.wikipedia.org/wiki/Hyalurononglucosaminidase Hyalurononglucosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.35 3.2.1.35] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Hyalurononglucosaminidase Hyalurononglucosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.35 3.2.1.35] </span> |
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2atm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2atm OCA], [http://www.ebi.ac.uk/pdbsum/2atm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2atm RCSB]</span> | ||
}} | }} | ||
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[[Category: Skov, L K.]] | [[Category: Skov, L K.]] | ||
[[Category: Spangfort, M D.]] | [[Category: Spangfort, M D.]] | ||
- | [[Category: MES]] | ||
- | [[Category: SO4]] | ||
[[Category: beta-alpha-barrel]] | [[Category: beta-alpha-barrel]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:57:08 2008'' |
Revision as of 22:57, 30 March 2008
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, resolution 2.000Å | |||||||
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Ligands: | , , | ||||||
Activity: | Hyalurononglucosaminidase, with EC number 3.2.1.35 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of the recombinant allergen Ves v 2
Overview
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.
About this Structure
2ATM is a Single protein structure of sequence from Vespula vulgaris. Full crystallographic information is available from OCA.
Reference
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
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