2ofz

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(New page: 200px<br /><applet load="2ofz" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ofz, resolution 1.17&Aring;" /> '''Ultrahigh Resolution...)
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[[Image:2ofz.jpg|left|200px]]<br /><applet load="2ofz" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ofz.jpg|left|200px]]<br /><applet load="2ofz" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ofz, resolution 1.17&Aring;" />
caption="2ofz, resolution 1.17&Aring;" />
'''Ultrahigh Resolution Crystal Structure of RNA Binding Domain of SARS Nucleopcapsid (N Protein) at 1.1 Angstrom Resolution in Monoclinic Form.'''<br />
'''Ultrahigh Resolution Crystal Structure of RNA Binding Domain of SARS Nucleopcapsid (N Protein) at 1.1 Angstrom Resolution in Monoclinic Form.'''<br />
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==About this Structure==
==About this Structure==
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2OFZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus] with EDO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OFZ OCA].
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2OFZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus] with <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OFZ OCA].
==Reference==
==Reference==
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[[Category: sars-orf9a]]
[[Category: sars-orf9a]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:09:41 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:56:37 2008''

Revision as of 11:56, 23 January 2008


2ofz, resolution 1.17Å

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Ultrahigh Resolution Crystal Structure of RNA Binding Domain of SARS Nucleopcapsid (N Protein) at 1.1 Angstrom Resolution in Monoclinic Form.

Overview

Conserved among all coronaviruses are four structural proteins: the matrix, (M), small envelope (E), and spike (S) proteins that are embedded in the, viral membrane and the nucleocapsid phosphoprotein (N), which exists in a, ribonucleoprotein complex in the lumen. The N-terminal domain of, coronaviral N proteins (N-NTD) provides a scaffold for RNA binding, while, the C-terminal domain (N-CTD) mainly acts as oligomerization modules, during assembly. The C terminus of the N protein anchors it to the viral, membrane by associating with M protein. We characterized the structures of, N-NTD from severe acute respiratory syndrome coronavirus (SARS-CoV) in two, crystal forms, at 1.17 A (monoclinic) and at 1.85 A (cubic), respectively, resolved by molecular replacement using the homologous avian infectious, bronchitis virus (IBV) structure. Flexible loops in the solution structure, of SARS-CoV N-NTD are now shown to be well ordered around the beta-sheet, core. The functionally important positively charged beta-hairpin protrudes, out of the core, is oriented similarly to that in the IBV N-NTD, and is, involved in crystal packing in the monoclinic form. In the cubic form, the, monomers form trimeric units that stack in a helical array. Comparison of, crystal packing of SARS-CoV and IBV N-NTDs suggests a common mode of RNA, recognition, but they probably associate differently in vivo during the, formation of the ribonucleoprotein complex. Electrostatic potential, distribution on the surface of homology models of related coronaviral, N-NTDs suggests that they use different modes of both RNA recognition and, oligomeric assembly, perhaps explaining why their nucleocapsids have, different morphologies.

About this Structure

2OFZ is a Single protein structure of sequence from Sars coronavirus with as ligand. Full crystallographic information is available from OCA.

Reference

Ribonucleocapsid Formation of Severe Acute Respiratory Syndrome Coronavirus through Molecular Action of the N-Terminal Domain of N Protein., Saikatendu KS, Joseph JS, Subramanian V, Neuman BW, Buchmeier MJ, Stevens RC, Kuhn P, J Virol. 2007 Apr;81(8):3913-21. Epub 2007 Jan 17. PMID:17229691

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