4C5Q

measles virus phosphoprotein tetramerization domain

Summary for 4C5Q

• Entry DOI: 10.2210/pdb4c5q/pdb
• Descriptor: PHOSPHOPROTEIN (2 entities in total)
• Functional Keywords: viral protein, oligomerization domain
• Biological source: MEASLES VIRUS
• Total number of polymer chains: 8
• Total formula weight: 72458.48

Authors

Blocquel, D.,Habchi, J.,Durand, E.,Sevajol, M.,Ferron, F.,Papageorgiou, N.,Longhi, S. (deposition date: 2013-09-14, 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

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: 24914970
DOI: 10.1107/S139900471400234X

Experimental method

X-RAY DIFFRACTION (2.2 Å)