2ofz
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2ofz.jpg|left|200px]] | + | [[Image:2ofz.jpg|left|200px]] |
| - | + | ||
| - | '''Ultrahigh Resolution Crystal Structure of RNA Binding Domain of SARS Nucleopcapsid (N Protein) at 1.1 Angstrom Resolution in Monoclinic Form.''' | + | {{Structure |
| + | |PDB= 2ofz |SIZE=350|CAPTION= <scene name='initialview01'>2ofz</scene>, resolution 1.17Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= N ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=227859 SARS coronavirus]) | ||
| + | }} | ||
| + | |||
| + | '''Ultrahigh Resolution Crystal Structure of RNA Binding Domain of SARS Nucleopcapsid (N Protein) at 1.1 Angstrom Resolution in Monoclinic Form.''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2OFZ is a [ | + | 2OFZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OFZ OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17229691 17229691] |
[[Category: Sars coronavirus]] | [[Category: Sars coronavirus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 25: | Line 34: | ||
[[Category: sars-orf9a]] | [[Category: sars-orf9a]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:59:15 2008'' |
Revision as of 15:59, 20 March 2008
| |||||||
| , resolution 1.17Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | N (SARS coronavirus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 17:59:15 2008
