PDBsum entry 3k7b

Go to PDB code: 
protein Protein-protein interface(s) links
Viral protein PDB id
Protein chains
85 a.a. *
Waters ×42
* Residue conservation analysis
PDB id:
Name: Viral protein
Title: The structure of the poxvirus a33 protein reveals a dimer of type lectin-like domains.
Structure: Protein a33. Chain: a, b. Fragment: unp residues 90-185. Engineered: yes. Mutation: yes
Source: Vaccinia virus wr. Vacv. Organism_taxid: 10254. Strain: western reserve (wr). Gene: a33r, sall3r. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.10Å     R-factor:   0.218     R-free:   0.257
Authors: H.P.Su,D.N.Garboczi
Key ref: H.P.Su et al. (2010). The structure of the poxvirus A33 protein reveals a dimer of unique C-type lectin-like domains. J Virol, 84, 2502-2510. PubMed id: 20032175
12-Oct-09     Release date:   19-Jan-10    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P68617  (A33_VACCW) -  Protein A33
185 a.a.
85 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)


J Virol 84:2502-2510 (2010)
PubMed id: 20032175  
The structure of the poxvirus A33 protein reveals a dimer of unique C-type lectin-like domains.
H.P.Su, K.Singh, A.G.Gittis, D.N.Garboczi.
The 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.