1r4g
From Proteopedia
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Solution structure of the Sendai virus protein X C-subdomain
Overview
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.
About this Structure
1R4G is a Single protein structure of sequence from Sendai virus. Active as RNA-directed RNA polymerase, with EC number 2.7.7.48 Full crystallographic information is available from OCA.
Reference
Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution., Blanchard L, Tarbouriech N, Blackledge M, Timmins P, Burmeister WP, Ruigrok RW, Marion D, Virology. 2004 Feb 20;319(2):201-11. PMID:14980481
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