7KD4

Structure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329 -388), fused to MBP. Space group P21.

7KD4 の概要

• エントリーDOI: 10.2210/pdb7kd4/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Maltodextrin-binding protein and Phosphoprotein fusion protein, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: paramyxovirus, pararubulavirus, rna-dependent rna polymerase, viral protein
• 由来する生物種: Serratia sp. (strain FS14); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96486.68

構造登録者

Webby, M.N.,Kingston, R.L. (登録日: 2020-10-08, 公開日: 2021-09-15, 最終更新日: 2023-10-18)

主引用文献

Webby, M.N.,Herr, N.,Bulloch, E.M.M.,Schmitz, M.,Keown, J.R.,Goldstone, D.C.,Kingston, R.L.
Structural Analysis of the Menangle Virus P Protein Reveals a Soft Boundary between Ordered and Disordered Regions.
Viruses, 13:-, 2021

PubMed Abstract: The paramyxoviral phosphoprotein (P protein) is the non-catalytic subunit of the viral RNA polymerase, and coordinates many of the molecular interactions required for RNA synthesis. All paramyxoviral P proteins oligomerize via a centrally located coiled-coil that is connected to a downstream binding domain by a dynamic linker. The C-terminal region of the P protein coordinates interactions between the catalytic subunit of the polymerase, and the viral nucleocapsid housing the genomic RNA. The inherent flexibility of the linker is believed to facilitate polymerase translocation. Here we report biophysical and structural characterization of the C-terminal region of the P protein from Menangle virus (MenV), a bat-borne paramyxovirus with zoonotic potential. The MenV P protein is tetrameric but can dissociate into dimers at sub-micromolar protein concentrations. The linker is globally disordered and can be modeled effectively as a worm-like chain. However, NMR analysis suggests very weak local preferences for alpha-helical and extended beta conformation exist within the linker. At the interface between the disordered linker and the structured C-terminal binding domain, a gradual disorder-to-order transition occurs, with X-ray crystallographic analysis revealing a dynamic interfacial structure that wraps the surface of the binding domain.

PubMed: 34578318
DOI: 10.3390/v13091737

実験手法

X-RAY DIFFRACTION (1.312 Å)