2Z7J

Structural insights into de multifunctional VP3 protein of birnaviruses:gold derivative

Summary for 2Z7J

• Entry DOI: 10.2210/pdb2z7j/pdb
• Related: 2R18
• Descriptor: Capsid assembly protein VP3, GOLD ION (3 entities in total)
• Functional Keywords: helix, capsid protein, hydrolase, protease, serine protease, virion, viral protein
• Biological source: Infectious bursal disease virus (Gumboro virus)
• Cellular location: Capsid protein VP2: Virion . Capsid protein VP3: Virion . Structural peptide 1: Virion . Structural peptide 2: Virion . Structural peptide 3: Virion . Structural peptide 4: Virion : P25220
• Total number of polymer chains: 1
• Total formula weight: 14880.92

Authors

Casanas, A.,Navarro, A.,Ferrer-Orta, C.,Gonzalez, D.,Rodriguez, J.F.,Verdaguer, N. (deposition date: 2007-08-23, release date: 2008-02-05, Last modification date: 2024-02-21)

Primary citation

Casanas, A.,Navarro, A.,Ferrer-Orta, C.,Gonzalez, D.,Rodriguez, J.F.,Verdaguer, N.
Structural insights into the multifunctional protein VP3 of birnaviruses.
Structure, 16:29-37, 2008

PubMed Abstract: Infectious bursal disease virus (IBDV), a member of the Birnaviridae family, is the causative agent of one of the most harmful poultry diseases. The IBDV genome encodes five mature proteins; of these, the multifunctional protein VP3 plays an essential role in virus morphogenesis. This protein, which interacts with the structural protein VP2, with the double-stranded RNA genome, and with the virus-encoded, RNA-dependent RNA polymerase, VP1, is involved not only in the formation of the viral capsid, but also in the recruitment of VP1 into the capsid and in the encapsidation of the viral genome. Here, we report the X-ray structure of the central region of VP3, residues 92-220, consisting of two alpha-helical domains connected by a long and flexible hinge that are organized as a dimer. Unexpectedly, the overall fold of the second VP3 domain shows significant structural similarities with different transcription regulation factors.

PubMed: 18184581
DOI: 10.1016/j.str.2007.10.023

Experimental method

X-RAY DIFFRACTION (2.4 Å)