2XGK
Virus like particle of L172W mutant of Minute Virus of Mice - the immunosuppressive strain
Summary for 2XGK
| Entry DOI | 10.2210/pdb2xgk/pdb |
| Related | 1MVM 1Z1C |
| Descriptor | COAT PROTEIN VP2 (1 entity in total) |
| Functional Keywords | virus, vlp, parvovirus |
| Biological source | MURINE MINUTE VIRUS |
| Total number of polymer chains | 1 |
| Total formula weight | 64818.66 |
| Authors | Plevka, P.,Hafenstein, S.,Tattersall, P.,Cotmore, S.,Farr, G.,D'Abramo, A.,Rossmann, M.G. (deposition date: 2010-06-04, release date: 2011-04-20, Last modification date: 2023-12-20) |
| Primary citation | Plevka, P.,Hafenstein, S.,Li, L.,D'Abrgamo, A.,Cotmore, S.F.,Rossmann, M.G.,Tattersall, P. Structure of a Packaging-Defective Mutant of Minute Virus of Mice Indicates that the Genome is Packaged Via a Pore at a 5-Fold Axis. J.Virol., 85:4822-, 2011 Cited by PubMed Abstract: The parvovirus minute virus of mice (MVM) packages a single copy of its linear single-stranded DNA genome into preformed capsids, in a process that is probably driven by a virus-encoded helicase. Parvoviruses have a roughly cylindrically shaped pore that surrounds each of the 12 5-fold vertices. The pore, which penetrates the virion shell, is created by the juxtaposition of 10 antiparallel β-strands, two from each of the 5-fold-related capsid proteins. There is a bottleneck in the channel formed by the symmetry-related side chains of the leucines at position 172. We report here the X-ray crystal structure of the particles produced by a leucine-to-tryptophan mutation at position 172 and the analysis of its biochemical properties. The mutant capsid had its 5-fold channel blocked, and the particles were unable to package DNA, strongly suggesting that the 5-fold pore is the packaging portal for genome entry. PubMed: 21367911DOI: 10.1128/JVI.02598-10 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.2 Å) |
Structure validation
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