2bxx
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(New page: 200px<br /><applet load="2bxx" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bxx, resolution 1.85Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 06:50, 21 November 2007
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CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF IBV CORONAVIRUS NUCLEOCAPSID. NATIVE CRYSTAL FORM
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
2BXX 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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