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2btl
From Proteopedia
(New page: 200px<br /><applet load="2btl" size="450" color="white" frame="true" align="right" spinBox="true" caption="2btl, resolution 1.95Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:2btl.gif|left|200px]]<br /><applet load="2btl" size=" | + | [[Image:2btl.gif|left|200px]]<br /><applet load="2btl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2btl, resolution 1.95Å" /> | caption="2btl, resolution 1.95Å" /> | ||
'''CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF IBV CORONAVIRUS NUCLEOCAPSID'''<br /> | '''CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF IBV CORONAVIRUS NUCLEOCAPSID'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The coronavirus nucleocapsid (N) protein packages viral genomic RNA into a | + | The coronavirus nucleocapsid (N) protein packages viral genomic RNA into a ribonucleoprotein complex. Interactions between N proteins and RNA are thus crucial for the assembly of infectious virus particles. The 45 kDa recombinant nucleocapsid N protein of coronavirus infectious bronchitis virus (IBV) is highly sensitive to proteolysis. We obtained a stable fragment of 14.7 kDa spanning its N-terminal residues 29-160 (IBV-N29-160). Like the N-terminal RNA binding domain (SARS-N45-181) of the severe acute respiratory syndrome virus (SARS-CoV) N protein, the crystal structure of the IBV-N29-160 fragment at 1.85 A resolution reveals a protein core composed of a five-stranded antiparallel beta sheet with a positively charged beta hairpin extension and a hydrophobic platform that are probably involved in RNA binding. Crosslinking studies demonstrate the formation of dimers, tetramers, and higher multimers of IBV-N. A model for coronavirus shell formation is proposed in which dimerization of the C-terminal domain of IBV-N leads to oligomerization of the IBV-nucleocapsid protein and viral RNA condensation. |
==About this Structure== | ==About this Structure== | ||
| - | 2BTL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Infectious_bronchitis_virus Infectious bronchitis virus]. Full crystallographic information is available from [http:// | + | 2BTL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Infectious_bronchitis_virus Infectious bronchitis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BTL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Fan, H.]] | [[Category: Fan, H.]] | ||
[[Category: Lescar, J.]] | [[Category: Lescar, J.]] | ||
| - | [[Category: Liu, D | + | [[Category: Liu, D X.]] |
[[Category: Ooi, A.]] | [[Category: Ooi, A.]] | ||
[[Category: nucleocapsid protein]] | [[Category: nucleocapsid protein]] | ||
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[[Category: viral nucleoprotein]] | [[Category: viral nucleoprotein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:41:28 2008'' |
Revision as of 14:41, 21 February 2008
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CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF IBV CORONAVIRUS NUCLEOCAPSID
Overview
The coronavirus nucleocapsid (N) protein packages viral genomic RNA into a ribonucleoprotein complex. Interactions between N proteins and RNA are thus crucial for the assembly of infectious virus particles. The 45 kDa recombinant nucleocapsid N protein of coronavirus infectious bronchitis virus (IBV) is highly sensitive to proteolysis. We obtained a stable fragment of 14.7 kDa spanning its N-terminal residues 29-160 (IBV-N29-160). Like the N-terminal RNA binding domain (SARS-N45-181) of the severe acute respiratory syndrome virus (SARS-CoV) N protein, the crystal structure of the IBV-N29-160 fragment at 1.85 A resolution reveals a protein core composed of a five-stranded antiparallel beta sheet with a positively charged beta hairpin extension and a hydrophobic platform that are probably involved in RNA binding. Crosslinking studies demonstrate the formation of dimers, tetramers, and higher multimers of IBV-N. A model for coronavirus shell formation is proposed in which dimerization of the C-terminal domain of IBV-N leads to oligomerization of the IBV-nucleocapsid protein and viral RNA condensation.
About this Structure
2BTL is a Single protein structure of sequence from Infectious bronchitis virus. Full crystallographic information is available from OCA.
Reference
The nucleocapsid protein of coronavirus infectious bronchitis virus: crystal structure of its N-terminal domain and multimerization properties., Fan H, Ooi A, Tan YW, Wang S, Fang S, Liu DX, Lescar J, Structure. 2005 Dec;13(12):1859-68. PMID:16338414
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