The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus-like structure.
We have employed NMR to investigate the structure of SARS coronavirus nucleocapsid protein dimer. We found that the secondary structure of the dimerization domain consists of five alpha helices and a beta-hairpin. The dimer interface consists of a continuous four-stranded beta-sheet superposed by two long alpha helices, reminiscent of that found in the nucleocapsid protein of porcine respiratory and reproductive syndrome virus. Extensive hydrogen bond formation between the two hairpins and hydrophobic interactions between the beta-sheet and the alpha helices render the interface highly stable. Sequence alignment suggests that other coronavirus may share the same structural topology.
Chang
Chung-ke
CK
Institute of Biomedical Sciences, Academia Sinica, Nankang, Taipei, Taiwan, ROC.
Sue
Shih-Che
SC
Yu
Tsan-hung
TH
Hsieh
Chiu-Min
CM
Tsai
Cheng-Kun
CK
Chiang
Yen-Chieh
YC
Lee
Shin-jye
SJ
Hsiao
Hsin-Hao
HH
Wu
Wen-Jin
WJ
Chang
Chi-Fon
CF
Huang
Tai-huang
TH
D000595:Amino Acid Sequence; D000818:Animals; D000086462:Coronavirus Nucleocapsid Proteins; D019281:Dimerization; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D019590:Nucleocapsid Proteins / Q000737:chemistry*; D019316:Porcine respiratory and reproductive syndrome virus / Q000737:chemistry; D017433:Protein Structure, Secondary; D045473:Severe acute respiratory syndrome-related coronavirus / Q000737:chemistry; D016415:Sequence Alignment
D000086462:Coronavirus Nucleocapsid Proteins; D019590:Nucleocapsid Proteins