7KD4
Structure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329 -388), fused to MBP. Space group P21.
Summary for 7KD4
| Entry DOI | 10.2210/pdb7kd4/pdb |
| Related PRD ID | PRD_900001 |
| Descriptor | Maltodextrin-binding protein and Phosphoprotein fusion protein, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | paramyxovirus, pararubulavirus, rna-dependent rna polymerase, viral protein |
| Biological source | Serratia sp. (strain FS14) More |
| Total number of polymer chains | 2 |
| Total formula weight | 96486.68 |
| Authors | Webby, M.N.,Kingston, R.L. (deposition date: 2020-10-08, release date: 2021-09-15, Last modification date: 2023-10-18) |
| Primary citation | 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 Cited by 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: 34578318DOI: 10.3390/v13091737 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.312 Å) |
Structure validation
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