1R4G

Solution structure of the Sendai virus protein X C-subdomain

Summary for 1R4G

• Entry DOI: 10.2210/pdb1r4g/pdb
• Descriptor: RNA polymerase alpha subunit (1 entity in total)
• Functional Keywords: three helix-bundle, viral protein, transferase
• Biological source: Sendai virus (strain Harris)
• Cellular location: Host cytoplasm: P04859
• Total number of polymer chains: 1
• Total formula weight: 5942.85

Authors

Blanchard, L.,Tarbouriech, N.,Blackledge, M.,Timmins, P.,Burmeister, W.P.,Ruigrok, R.W.,Marion, D. (deposition date: 2003-10-06, release date: 2004-03-09, Last modification date: 2024-05-22)

Primary citation

Blanchard, L.,Tarbouriech, N.,Blackledge, M.,Timmins, P.,Burmeister, W.P.,Ruigrok, R.W.,Marion, D.
Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution
Virology, 319:201-211, 2004

PubMed Abstract: 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.

PubMed: 14980481
DOI: 10.1016/j.virol.2003.10.029

Experimental method

SOLUTION NMR