1r4g

<StructureSection load='1r4g' size='340' side='right'caption='[[1r4g]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1r4g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sendh Sendh]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R4G FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">P ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11196 SENDH])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </span></td></tr>

[[https://www.uniprot.org/uniprot/PHOSP_SENDH PHOSP_SENDH]] Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template. Acts as a chaperone for newly synthesized free N protein, so-called N(0). Stabilizes the L protein upon binding it.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:14980481</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Blackledge, M]]

[[Category: Blanchard, L]]

[[Category: Burmeister, W P]]

[[Category: Marion, D]]

[[Category: Ruigrok, R W]]

[[Category: Tarbouriech, N]]

[[Category: Timmins, P]]

[[Category: Viral protein]]