2K7X
solution structure of C-terminal domain of SARS-CoV main protease
Summary for 2K7X
| Entry DOI | 10.2210/pdb2k7x/pdb |
| Descriptor | SARS-CoV main protease (1 entity in total) |
| Functional Keywords | solution structure, c-terminal domain, main protease, hydrolase |
| Biological source | SARS coronavirus |
| Total number of polymer chains | 1 |
| Total formula weight | 13282.98 |
| Authors | |
| Primary citation | Zhong, N.,Zhang, S.,Xue, F.,Kang, X.,Zou, P.,Chen, J.,Liang, C.,Rao, Z.,Jin, C.,Lou, Z.,Xia, B. C-terminal domain of SARS-CoV main protease can form a 3D domain-swapped dimer. Protein Sci., 18:839-844, 2009 Cited by PubMed Abstract: SARS coronavirus main protease (M(pro)) plays an essential role in the extensive proteolytic processing of the viral polyproteins (pp1a and pp1ab), and it is an important target for anti-SARS drug development. We have reported that both the M(pro) C-terminal domain alone (M(pro)-C) and the N-finger deletion mutant of M(pro) (M(pro)-Delta7) exist as a stable dimer and a stable monomer (Zhong et al., J Virol 2008; 82:4227-4234). Here, we report structures of both M(pro)-C monomer and dimer. The structure of the M(pro)-C monomer is almost identical to that of the C-terminal domain in the crystal structure of M(pro). Interestingly, the M(pro)-C dimer structure is characterized by 3D domain-swapping, in which the first helices of the two protomers are interchanged and each is enwrapped by four other helices from the other protomer. Each folding subunit of the M(pro)-C domain-swapped dimer still has the same general fold as that of the M(pro)-C monomer. This special dimerization elucidates the structural basis for the observation that there is no exchange between monomeric and dimeric forms of M(pro)-C and M(pro)-Delta7. PubMed: 19319935DOI: 10.1002/pro.76 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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