4HEO

Hendra virus Phosphoprotein C terminal domain

4HEO の概要

• エントリーDOI: 10.2210/pdb4heo/pdb
• 分子名称: Phosphoprotein, CHLORIDE ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: viral polymerase cofactor, phosphoprotein, viral protein
• 由来する生物種: Hendra virus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 15397.75

構造登録者

Yabukarski, F.,Tarbouriech, N.,Jamin, M. (登録日: 2012-10-04, 公開日: 2013-10-09, 最終更新日: 2024-11-06)

主引用文献

Communie, G.,Habchi, J.,Yabukarski, F.,Blocquel, D.,Schneider, R.,Tarbouriech, N.,Papageorgiou, N.,Ruigrok, R.W.,Jamin, M.,Jensen, M.R.,Longhi, S.,Blackledge, M.
Atomic Resolution Description of the Interaction between the Nucleoprotein and Phosphoprotein of Hendra Virus.
Plos Pathog., 9:e1003631-e1003631, 2013

PubMed Abstract: Hendra virus (HeV) is a recently emerged severe human pathogen that belongs to the Henipavirus genus within the Paramyxoviridae family. The HeV genome is encapsidated by the nucleoprotein (N) within a helical nucleocapsid. Recruitment of the viral polymerase onto the nucleocapsid template relies on the interaction between the C-terminal domain, N(TAIL), of N and the C-terminal X domain, XD, of the polymerase co-factor phosphoprotein (P). Here, we provide an atomic resolution description of the intrinsically disordered N(TAIL) domain in its isolated state and in intact nucleocapsids using nuclear magnetic resonance (NMR) spectroscopy. Using electron microscopy, we show that HeV nucleocapsids form herringbone-like structures typical of paramyxoviruses. We also report the crystal structure of XD of P that consists of a three-helix bundle. We study the interaction between N(TAIL) and XD using NMR titration experiments and provide a detailed mapping of the reciprocal binding sites. We show that the interaction is accompanied by α-helical folding of the molecular recognition element of N(TAIL) upon binding to a hydrophobic patch on the surface of XD. Finally, using solution NMR, we investigate the interaction between intact nucleocapsids and XD. Our results indicate that monomeric XD binds to N(TAIL) without triggering an additional unwinding of the nucleocapsid template. The present results provide a structural description at the atomic level of the protein-protein interactions required for transcription and replication of HeV, and the first direct observation of the interaction between the X domain of P and intact nucleocapsids in Paramyxoviridae.

PubMed: 24086133
DOI: 10.1371/journal.ppat.1003631

実験手法

X-RAY DIFFRACTION (1.65 Å)