2INY
Nanoporous Crystals of Chicken Embryo Lethal Orphan (CELO) Adenovirus Major Coat Protein, Hexon
Summary for 2INY
| Entry DOI | 10.2210/pdb2iny/pdb |
| Related | 1HX6 1M3Y 1P2Z 1P30 2BBD |
| Descriptor | Hexon protein (1 entity in total) |
| Functional Keywords | avian adenovirus, celo, major coat protein, hexon, crystal packing, nanotechnology, viral jelly roll, viral protein |
| Biological source | Fowl adenovirus 1 |
| Cellular location | Virion : P42671 |
| Total number of polymer chains | 1 |
| Total formula weight | 106795.63 |
| Authors | Xu, L.,Benson, S.D.,Burnett, R.M. (deposition date: 2006-10-09, release date: 2007-02-06, Last modification date: 2023-08-30) |
| Primary citation | Xu, L.,Benson, S.D.,Burnett, R.M. Nanoporous crystals of chicken embryo lethal orphan (CELO) adenovirus major coat protein, hexon. J.Struct.Biol., 157:424-431, 2007 Cited by PubMed Abstract: CELO (chicken embryo lethal orphan) virus is an avian adenovirus that is being developed as a gene transfer vector. Its trimeric major coat protein (942 residues, 106,709 Da) has 42% sequence identity to human adenovirus type 2 (AdH2) hexon and 45% to AdH5 hexon. For structural studies, the growth of CELO virus has been optimized, and its hexon purified and crystallized. The hexon crystals, the first non-human example, diffract to 3.9 A resolution. Molecular replacement using the AdH5 model was used to identify the location of the CELO hexon within the unit cell. There is one hexon monomer in the asymmetric unit of the trigonal space group P321 (a=b=157.8 A, c=114.2 A, gamma=120 degrees) and the solvent content is 67.8%. The hexons pack in a hexagonal honeycomb so that large approximately 100 A diameter channels run through the entire crystal. This remarkable property of the crystals lends itself to their exploitation as a nanomaterial. Structural studies on CELO will elucidate the differences between avian and human adenoviruses and contribute to a better understanding of adenoviruses with non-human hosts. PubMed: 17071105DOI: 10.1016/j.jsb.2006.08.017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.9 Å) |
Structure validation
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