2BTL

Crystal structure of the N-terminal domain of IBV coronavirus nucleocapsid

Summary for 2BTL

• Entry DOI: 10.2210/pdb2btl/pdb
• Related: 2BXX
• Descriptor: INFECTIOUS BRONCHITIS VIRUS NUCLEOCAPSID PROTEIN (2 entities in total)
• Functional Keywords: nucleocapsid protein, phosphorylation, rna-binding, viral nucleoprotein
• Biological source: AVIAN INFECTIOUS BRONCHITIS VIRUS
• Cellular location: Virion (By similarity): P69596
• Total number of polymer chains: 2
• Total formula weight: 30165.38

Authors

Fan, H.,Ooi, A.,Liu, D.-X.,Lescar, J. (deposition date: 2005-06-03, release date: 2005-12-14, Last modification date: 2024-05-08)

Primary citation

Fan, H.,Ooi, A.,Tan, Y.W.,Wang, S.,Fang, S.,Liu, D.-X.,Lescar, J.
The Nucleocapsid Protein of Coronavirus Infectious Bronchitis Virus: Crystal Structure of its N-Terminal Domain and Multimerization Properties.
Structure, 13:1859-, 2005

PubMed Abstract: 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.

PubMed: 16338414
DOI: 10.1016/J.STR.2005.08.021

Experimental method

X-RAY DIFFRACTION (1.95 Å)