5CDD
Crystal Structure of Israel acute Paralysis Virus Pentamer
Summary for 5CDD
| Entry DOI | 10.2210/pdb5cdd/pdb |
| Descriptor | Structural polyprotein, VP1, Structural polyprotein, VP3, Structural polyprotein, VP2, ... (4 entities in total) |
| Functional Keywords | pentamer, capsid, honeybee virus, pathogen, virus |
| Biological source | Israeli acute paralysis virus More |
| Cellular location | Virion : B3TZF1 D1FK67 D1FK67 |
| Total number of polymer chains | 3 |
| Total formula weight | 79626.97 |
| Authors | Mullapudi, E.,Plevka, P. (deposition date: 2015-07-03, release date: 2016-07-06, Last modification date: 2024-05-08) |
| Primary citation | Kalynych, S.,Pridal, A.,Palkova, L.,Levdansky, Y.,de Miranda, J.R.,Plevka, P. Virion Structure of Iflavirus Slow Bee Paralysis Virus at 2.6-Angstrom Resolution. J.Virol., 90:7444-7455, 2016 Cited by PubMed Abstract: The western honeybee (Apis mellifera) is the most important commercial insect pollinator. However, bees are under pressure from habitat loss, environmental stress, and pathogens, including viruses that can cause lethal epidemics. Slow bee paralysis virus (SBPV) belongs to the Iflaviridae family of nonenveloped single-stranded RNA viruses. Here we present the structure of the SBPV virion determined from two crystal forms to resolutions of 3.4 Å and 2.6 Å. The overall structure of the virion resembles that of picornaviruses, with the three major capsid proteins VP1 to 3 organized into a pseudo-T3 icosahedral capsid. However, the SBPV capsid protein VP3 contains a C-terminal globular domain that has not been observed in other viruses from the order Picornavirales The protruding (P) domains form "crowns" on the virion surface around each 5-fold axis in one of the crystal forms. However, the P domains are shifted 36 Å toward the 3-fold axis in the other crystal form. Furthermore, the P domain contains the Ser-His-Asp triad within a surface patch of eight conserved residues that constitutes a putative catalytic or receptor-binding site. The movements of the domain might be required for efficient substrate cleavage or receptor binding during virus cell entry. In addition, capsid protein VP2 contains an RGD sequence that is exposed on the virion surface, indicating that integrins might be cellular receptors of SBPV. PubMed: 27279610DOI: 10.1128/JVI.00680-16 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
Download full validation report
