2W2R

Structure of the vesicular stomatitis virus matrix protein

Summary for 2W2R

• Entry DOI: 10.2210/pdb2w2r/pdb
• Related: 2W2S
• Descriptor: MATRIX PROTEIN (2 entities in total)
• Functional Keywords: viral assembly, viral morphogenesis, vsv, polymer, viral protein, matrix protein
• Biological source: VESICULAR STOMATITIS VIRUS
• Total number of polymer chains: 1
• Total formula weight: 26525.03

Authors

Graham, S.C.,Assenberg, R.,Delmas, O.,Verma, A.,Gholami, A.,Talbi, C.,Owens, R.J.,Stuart, D.I.,Grimes, J.M.,Bourhy, H. (deposition date: 2008-11-03, release date: 2009-01-13, Last modification date: 2024-10-09)

Primary citation

Graham, S.C.,Assenberg, R.,Delmas, O.,Verma, A.,Gholami, A.,Talbi, C.,Owens, R.J.,Stuart, D.I.,Grimes, J.M.,Bourhy, H.
Rhabdovirus Matrix Protein Structures Reveal a Novel Mode of Self-Association.
Plos Pathog., 4:251-, 2008

PubMed Abstract: The matrix (M) proteins of rhabdoviruses are multifunctional proteins essential for virus maturation and budding that also regulate the expression of viral and host proteins. We have solved the structures of M from the vesicular stomatitis virus serotype New Jersey (genus: Vesiculovirus) and from Lagos bat virus (genus: Lyssavirus), revealing that both share a common fold despite sharing no identifiable sequence homology. Strikingly, in both structures a stretch of residues from the otherwise-disordered N terminus of a crystallographically adjacent molecule is observed binding to a hydrophobic cavity on the surface of the protein, thereby forming non-covalent linear polymers of M in the crystals. While the overall topology of the interaction is conserved between the two structures, the molecular details of the interactions are completely different. The observed interactions provide a compelling model for the flexible self-assembly of the matrix protein during virion morphogenesis and may also modulate interactions with host proteins.

PubMed: 19112510
DOI: 10.1371/JOURNAL.PPAT.1000251

Experimental method

X-RAY DIFFRACTION (1.83 Å)