2YGC
Structure of vaccinia virus D13 scaffolding protein
Summary for 2YGC
| Entry DOI | 10.2210/pdb2ygc/pdb |
| Related | 2YGB |
| Descriptor | RIFAMPICIN RESISTANCE PROTEIN (2 entities in total) |
| Functional Keywords | viral protein, viral evolution |
| Biological source | VACCINIA VIRUS |
| Total number of polymer chains | 3 |
| Total formula weight | 192983.25 |
| Authors | Bahar, M.W.,Graham, S.C.,Stuart, D.I.,Grimes, J.M. (deposition date: 2011-04-13, release date: 2011-07-20, Last modification date: 2024-11-20) |
| Primary citation | Bahar, M.W.,Graham, S.C.,Stuart, D.I.,Grimes, J.M. Insights Into the Evolution of a Complex Virus from the Crystal Structure of Vaccinia Virus D13. Structure, 19:1011-, 2011 Cited by PubMed Abstract: The morphogenesis of poxviruses such as vaccinia virus (VACV) sees the virion shape mature from spherical to brick-shaped. Trimeric capsomers of the VACV D13 protein form a transitory, stabilizing lattice on the surface of the initial spherical immature virus particle. The crystal structure of D13 reveals that this major scaffolding protein comprises a double β barrel "jelly-roll" subunit arranged as pseudo-hexagonal trimers. These structural features are characteristic of the major capsid proteins of a lineage of large icosahedral double-stranded DNA viruses including human adenovirus and the bacteriophages PRD1 and PM2. Structure-based phylogenetic analysis confirms that VACV belongs to this lineage, suggesting that (analogously to higher organism embryogenesis) early poxvirus morphogenesis reflects their evolution from a lineage of viruses sharing a common icosahedral ancestor. PubMed: 21742267DOI: 10.1016/J.STR.2011.03.023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.02 Å) |
Structure validation
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