2W2S

Structure of the Lagos bat virus matrix protein

2W2S の概要

• エントリーDOI: 10.2210/pdb2w2s/pdb
• 関連するPDBエントリー: 2W2R
• 分子名称: MATRIX PROTEIN (1 entity in total)
• 機能のキーワード: viral assembly, viral morphogenesis, lagos bat virus, polymer, viral protein, matrix protein, vsv
• 由来する生物種: LAGOS BAT VIRUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23177.53

構造登録者

Graham, S.C.,Assenberg, R.,Delmas, O.,Verma, A.,Gholami, A.,Talbi, C.,Owens, R.J.,Stuart, D.I.,Grimes, J.M.,Bourhy, H. (登録日: 2008-11-03, 公開日: 2009-01-13, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.75 Å)