Without its N-finger, the main protease of severe acute respiratory syndrome coronavirus can form a novel dimer through its C-terminal domain

Journal of Virology

Volumn 82, Issue 9, 2008, Pages 4227-4234

  Zhong, Nan ^a,b   Zhang, Shengnan ^a,b   Zou, Peng ^a,b   Chen, Jiaxuan ^a   Kang, Xue ^a,b   Li, Zhe ^a   Liang, Chao ^a   Jin, Changwen ^a,b   Xia, Bin ^a,b  

^a PEKING UNIVERSITY   (China)

^b PEKING UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

POLYPROTEIN; PROTEINASE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; DIMERIZATION; ENZYME ACTIVITY; ESCHERICHIA COLI; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; ROOM TEMPERATURE; SARS CORONAVIRUS;

CLONING, MOLECULAR; DIMERIZATION; ESCHERICHIA COLI; PEPTIDE HYDROLASES; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, TERTIARY; PROVIRUSES; SARS VIRUS; SEQUENCE DELETION;

ESCHERICHIA COLI; SARS CORONAVIRUS;

EID: 42449143874     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.02612-07     Document Type: Article

References (30)

1. Anand, K., G. J. Palm, J. R. Mesters, S. G. Siddell, J. Ziebuhr, and R. Hilgenfeld. 2002. Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain. EMBO J. 21:3213-3224.
2. Anand, K., J. Ziebuhr, P. Wadhwani, J. R. Mesters, and R. Hilgenfeld. 2003. Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs. Science 300:1763-1767.
3. Chan, H. L., S. K. Tsui, and J. J. Sung. 2003. Coronavirus in severe acute respiratory syndrome (SARS). Trends Mol. Med. 9:323-325.
4. Chen, S., L. Chen, J. Tan, J. Chen, L. Du, T. Sun, J. Shen, K. Chen, H. Jiang, and X. Shen. 2005. Severe acute respiratory syndrome coronavirus 3C-like proteinase N terminus is indispensable for proteolytic activity but not for enzyme dimerization. Biochemical and thermodynamic investigation in conjunction with molecular dynamics simulations. J. Biol. Chem. 280:164-173.
5. Chen, S., T. Hu, J. Zhang, J. Chen, K. Chen, J. Ding, H. Jiang, and X. Shen. 2008. Mutation of Gly11 on the dimer interface results in the complete crystallographic dimer dissociation of SARS-CoV 3CLpro: crystal structure with molecular dynamics simulations. J. Biol. Chem. 283:554-564.
6. Chou, C. Y., H. C. Chang, W. C. Hsu, T. Z. Lin, C. H. Lin, and G. G. Chang. 2004. Quaternary structure of the severe acute respiratory syndrome (SARS) coronavirus main protease. Biochemistry 43:14958-14970.
7. Delaglio, F., S. Grzesiek, G. W. Vuister, G. Zhu, J. Pfeifer, and A. Bax. 1995. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6:277-293.
8. Dominguez, C., R. Boelens, and A. M. Bonvin. 2003. HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. J. Am. Chem. Soc. 125:1731-1737.
9. Fan, K., P. Wei, Q. Feng, S. Chen, C. Huang, L. Ma, B. Lai, J. Pei, Y. Liu, J. Chen, and L. Lai. 2004. Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase. J. Biol. Chem. 279:1637-1642.
10. Graziano, V., W. J. McGrath, L. Yang, and W. F. Mangel. 2006. SARS CoV main proteinase: the monomer-dimer equilibrium dissociation constant. Biochemistry 45:14632-14641.
11. Hsu, W. C., H. C. Chang, C. Y. Chou, P. J. Tsai, P. I. Lin, and G. G. Chang. 2005. Critical assessment of important regions in the subunit association and catalytic action of the severe acute respiratory syndrome coronavirus main protease. J. Biol. Chem. 280:22741-22748.
12. Johnson, B. A., and R. A. Blevins. 1994. NMR View: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4:603-614.
13. Koradi, R., M. Billeter, and K. Wuthrich. 1996. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:51-55, 29-32.
14. Kuiken, T., R. A. Fouchier, M. Schutten, G. F. Rimmelzwaan, G. van Amerongen, D. van Riel, J. D. Laman, T. de Jong, G. van Doornum, W. Lim, A. E. Ling, P. K. Chan, J. S. Tam, M. C. Zambon, R. Gopal, C. Drosten, S. van der Werf, N. Escriou, J. C. Manuguerra, K. Stohr, J. S. Peiris, and A. D. Osterhaus. 2003. Newly discovered coronavirus as the primary cause of severe acute respiratory syndrome. Lancet 362:263-270.
15. Lee, T. W., M. M. Cherney, C. Huitema, J. Liu, K. E. James, J. C. Powers, L. D. Eltis, and M. N. James. 2005. Crystal structures of the main peptidase from the SARS coronavirus inhibited by a substrate-like aza-peptide epoxide. J. Mol. Biol. 353:1137-1151.
16. Leng, Q., and Z. Bentwich. 2003. A novel coronavirus and SARS. New Engl. J. Med. 349:709.
17. Marra, M. A., S. J. Jones, C. R. Astell, R. A. Holt, A. Brooks-Wilson, Y. S. Butterfield, J. Khattra, J. K. Asano, S. A. Barber, S. Y. Chan, A. Cloutier, S. M. Coughlin, D. Freeman, N. Girn, O. L. Griffith, S. R. Leach, M. Mayo, H. McDonald, S. B. Montgomery, P. K. Pandoh, A. S. Petrescu, A. G. Robertson, J. E. Schein, A. Siddiqui, D. E. Smailus, J. M. Stott, G. S. Yang, F. Plummer, A. Andonov, H. Artsob, N. Bastien, K. Bernard, T. F. Booth, D. Bowness, M. Czub, M. Drebot, L. Fernando, R. Flick, M. Garbutt, M. Gray, A. Grolla, S. Jones, H. Feldmann, A. Meyers, A. Kabani, Y. Li, S. Normand, U. Stroher, G. A. Tipples, S. Tyler, R. Vogrig, D. Ward, B. Watson, R. C. Brunham, M. Krajden, M. Petric, D. M. Skowronski, C. Upton, and R. L. Roper. 2003. The genome sequence of the SARS-associatcd coronavirus. Science 300:1399-1404.
18. Mulder, F. A., D. Schipper, R. Bott, and R. Boelens. 1999. Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins. J. Mol. Biol. 292:111-123.
19. Rota, P. A., M. S. Oberste, S. S. Monroe, W. A. Nix, R. Campagnoli, J. P. Icenogle, S. Penaranda, B. Bankamp, K. Maher, M. H. Chen, S. Tong, A. Tamin, L. Lowe, M. Frace, J. L. DeRisi, Q. Chen, D. Wang, D. D. Erdman, T. C. Peret, C. Burns, T. G. Ksiazek, P. E. Rollin, A. Sanchez, S. Liffick, B. Holloway, J. Limor, K. McCaustland, M. Olsen-Rasmussen, R. Fouchier, S. Gunther, A. D. Osterhaus, C. Drosten, M. A. Pallansch, L. J. Anderson, and W. J. Bellini. 2003. Characterization of a novel coronavirus associated with severe acute respiratory syndrome. Science 300:1394-1399.
20. Ruan, Y. J., C. L. Wei, A. L. Ee, V. B. Vega, H. Thoreau, S. T. Su, J. M. Chia, P. Ng, K. P. Chiu, L. Lim, T. Zhang, C. K. Peng, E. O. Lin, N. M. Lee, S. L. Yee, L. F. Ng, R. E. Chee, L. W. Stanton, P. M. Long, and E. T. Liu. 2003. Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection. Lancet 361:1779-1785.
21. Sattler, M., J. Schleucher, and C. Griesinger. 1999. Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog. Nucl. Magn. Reson. Spectrosc. 34:93-158.
22. Shi, J., Z. Wei, and J. Song. 2004. Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme: defining the extra domain as a new target for design of highly specific protease inhibitors. J. Biol. Chem. 279:24765-24773.
23. Tan, J., K. H. Verschueren, K. Anand, J. Shen, M. Yang, Y. Xu, Z. Rao, J. Bigalke, B. Heisen, J. R. Mesters, K. Chen, X. Shen, H. Jiang, and R. Hilgenfeld. 2005. pH-dependent conformational flexibility of the SARS-CoV main proteinase (M(pro)) dimer: molecular dynamics simulations and multiple X-ray structure analyses. J. Mol. Biol. 354:25-40.
24. Wei, P., K. Fan, H. Chen, L. Ma, C. Huang, L. Tan, D. Xi, C. Li, Y. Liu, A. Cao, and L. Lai. 2006. The N-terminal octapeptide acts as a dimerization inhibitor of SARS coronavirus 3C-like proteinase. Biochem. Biophys. Res. Commun. 339:865-872.
25. World Health Organization. 2003. SARS outbreak contained worldwide. World Health Organization, Geneva, Switzerland. http://www.who.int/ mediacentre/news/releases/2003/pr56/en/.
26. Wishart, D. S., C. G. Bigam, J. Yao, F. Abildgaard, H. J. Dyson, E. Oldfield, J. L. Markley, and B. D. Sykes. 1995. 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J. Biomol. NMR 6:135-140.
27. Xu, T., A. Ooi, H. C. Lee, R. Wilmouth, D. X. Liu, and J. Lescar. 2005. Structure of the SARS coronavirus main proteinase as an active C2 crystallography dimer. Acta Crystallogr. F 61:964-966.
28. Xue, X., H. Yang, W. Shen, Q. Zhao, J. Li, K. Yang, C. Chen, Y. Jin, M. Bartlam, and Z. Rao. 2007. Production of authentic SARS-CoV M(pro) with enhanced activity: application as a novel tag-cleavage endopeptidase for protein overproduction. J. Mol. Biol. 366:965-975.
29. Yang, H., W. Xie, X. Xue, K. Yang, J. Ma, W. Liang, Q. Zhao, Z. Zhou, D. Pei, J. Ziebuhr, R. Hilgenfeld, K. Y. Yuen, L. Wong, G. Gao, S. Chen, Z. Chen, D. Ma, M. Bartlam, and Z. Rao. 2005. Design of wide-spectrum inhibitors targeting coronavirus main proteases. PLoS Biol. 3:e324.
30. Yang, H., M. Yang, Y. Ding, Y. Liu, Z. Lou, Z. Zhou, L. Sun, L. Mo, S. Ye, H. Pang, G. F. Gao, K. Anand, M. Bartlam, B. Hilgenfeld, and Z. Rao. 2003. The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor. Proc. Natl. Acad. Sci. USA 100:13190-13195.