4BHV
Measles virus phosphoprotein tetramerization domain
Summary for 4BHV
Entry DOI | 10.2210/pdb4bhv/pdb |
Descriptor | PHOSPHOPROTEIN, ACETATE ION, CALCIUM ION, ... (4 entities in total) |
Functional Keywords | oligomerization domain, viral protein |
Biological source | MEASLES VIRUS |
Total number of polymer chains | 4 |
Total formula weight | 30298.19 |
Authors | Blocquel, D.,Habchi, J.,Durand, E.,Sevajol, M.,Ferron, F.,Papageorgiou, N.,Longhi, S. (deposition date: 2013-04-08, release date: 2014-04-09, Last modification date: 2023-12-20) |
Primary citation | Blocquel, D.,Habchi, J.,Durand, E.,Sevajol, M.,Ferron, F.,Erales, J.,Papageorgiou, N.,Longhi, S. Coiled-Coil Deformations in Crystal Structures: The Measles Virus Phosphoprotein Multimerization Domain as an Illustrative Example. Acta Crystallogr.,Sect.D, 70:1589-, 2014 Cited by PubMed Abstract: The structures of two constructs of the measles virus (MeV) phosphoprotein (P) multimerization domain (PMD) are reported and are compared with a third structure published recently by another group [Communie et al. (2013), J. Virol. 87, 7166-7169]. Although the three structures all have a tetrameric and parallel coiled-coil arrangement, structural comparison unveiled considerable differences in the quaternary structure and unveiled that the three structures suffer from significant structural deformation induced by intermolecular interactions within the crystal. These results show that crystal packing can bias conclusions about function and mechanism based on analysis of a single crystal structure, and they challenge to some extent the assumption according to which coiled-coil structures can be reliably predicted from the amino-acid sequence. Structural comparison also highlighted significant differences in the extent of disorder in the C-terminal region of each monomer. The differential flexibility of the C-terminal region is also supported by size-exclusion chromatography and small-angle X-ray scattering studies, which showed that MeV PMD exists in solution as a dynamic equilibrium between two tetramers of different compaction. Finally, the possible functional implications of the flexibility of the C-terminal region of PMD are discussed. PubMed: 24914970DOI: 10.1107/S139900471400234X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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