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1r4g
From Proteopedia
(New page: 200px<br /><applet load="1r4g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r4g" /> '''Solution structure of the Sendai virus prote...) |
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'''Solution structure of the Sendai virus protein X C-subdomain'''<br /> | '''Solution structure of the Sendai virus protein X C-subdomain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The RNA-dependent RNA polymerase of the Sendai virus (SeV) consists of the | + | 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== | ==About this Structure== | ||
| - | 1R4G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sendai_virus Sendai virus]. Active as [http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] Full crystallographic information is available from [http:// | + | 1R4G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sendai_virus Sendai virus]. Active as [http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4G OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Blackledge, M.]] | [[Category: Blackledge, M.]] | ||
[[Category: Blanchard, L.]] | [[Category: Blanchard, L.]] | ||
| - | [[Category: Burmeister, W | + | [[Category: Burmeister, W P.]] |
[[Category: Marion, D.]] | [[Category: Marion, D.]] | ||
| - | [[Category: Ruigrok, R | + | [[Category: Ruigrok, R W.]] |
[[Category: Tarbouriech, N.]] | [[Category: Tarbouriech, N.]] | ||
[[Category: Timmins, P.]] | [[Category: Timmins, P.]] | ||
[[Category: three helix-bundle]] | [[Category: three helix-bundle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:08 2008'' |
Revision as of 12:47, 21 February 2008
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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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