3k7b
The structure of the poxvirus A33 protein reveals a dimer of unique C-type lectin-like domains.
Structural highlights
FunctionPG161_VACCW Forms a complex with OPG162 and OPG190 to coordinate the incorporation of OPG164 into wrapped enveloped virion (EV) membranes and, subsequently, the production of actin tails (PubMed:11119600, PubMed:23255618, PubMed:31941777). Therefore plays an essential role in efficient cell-to-cell spread of viral particles.[1] [2] [3] [4] [5] 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 PubMedThe current vaccine against smallpox is an infectious form of vaccinia virus that has significant side effects. Alternative vaccine approaches using recombinant viral proteins are being developed. A target of subunit vaccine strategies is the poxvirus protein A33, a conserved protein in the Chordopoxvirinae subfamily of Poxviridae that is expressed on the outer viral envelope. Here we have determined the structure of the A33 ectodomain of vaccinia virus. The structure revealed C-type lectin-like domains (CTLDs) that occur as dimers in A33 crystals with five different crystal lattices. Comparison of the A33 dimer models shows that the A33 monomers have a degree of flexibility in position within the dimer. Structural comparisons show that the A33 monomer is a close match to the Link module class of CTLDs but that the A33 dimer is most similar to the natural killer (NK)-cell receptor class of CTLDs. Structural data on Link modules and NK-cell receptor-ligand complexes suggest a surface of A33 that could interact with viral or host ligands. The dimer interface is well conserved in all known A33 sequences, indicating an important role for the A33 dimer. The structure indicates how previously described A33 mutations disrupt protein folding and locates the positions of N-linked glycosylations and the epitope of a protective antibody. The structure of the poxvirus A33 protein reveals a dimer of unique C-type lectin-like domains.,Su HP, Singh K, Gittis AG, Garboczi DN J Virol. 2010 Mar;84(5):2502-10. Epub 2009 Dec 23. PMID:20032175[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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