Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution
| Autor: | Wilhelm P. Burmeister, Dominique Marion, Laurence Blanchard, Martin Blackledge, Nicolas Tarbouriech, Peter A. Timmins, Rob W.H. Ruigrok |
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| Rok vydání: | 2004 |
| Předmět: |
Models
Molecular Magnetic Resonance Spectroscopy EGF-like domain HMG-box Molecular Sequence Data Protein domain Immunoglobulin domain Biology RNA-dependent RNA polymerase Sendai virus Protein Structure Secondary HAMP domain Viral Proteins Virology Amino Acid Sequence B3 domain Nucleocapsid Phosphoproteins Molecular biology Protein Structure Tertiary Cyclic nucleotide-binding domain Phosphoprotein Partially unfolded protein Paramyxoviridae Biophysics NMR structure Sequence Alignment Binding domain |
| Zdroj: | Virology. 319:201-211 |
| ISSN: | 0042-6822 |
| DOI: | 10.1016/j.virol.2003.10.029 |
| Popis: | The RNA-dependent RNA polymerase of the Sendai virus (SeV) consists of the large protein (L) and the phosphoprotein (P). P plays a crucial role in the enzyme by positioning L (which carries the polymerase activity) onto the matrix for transcription and replication formed by the RNA and the nucleoprotein, the N-RNA. P has a modular structure with distinct functional domains: an N-terminal domain involved in binding to N degrees (N that is not yet bound to RNA) and a C-terminal domain that carries the oligomerisation domain, the N-RNA binding domain and the L binding domain and that, combined with L, is active in transcription. Structural data have previously been obtained on the N-terminal domain and on the oligomerisation domain of P, but not yet on its N-RNA binding domain (also-called the X protein). Here we present an NMR and a small angle neutron scattering study of the SeV X protein. We show that this molecule presents two subdomains linked by an 11-residue linker, with the N-subdomain lacking a well-defined conformation. The 3D structure of the C-subdomain consists of three alpha-helices revealing an asymmetric charge distribution that may be important for binding to RNA-bound nucleoprotein. The structure of the entire C-terminal domain of P is modelled from its constituent parts in combination with small angle scattering data on this domain. |
| Databáze: | OpenAIRE |
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