5LAC
SeMet Labeled Derivative of Cavally Virus 3CL Protease
Summary for 5LAC
| Entry DOI | 10.2210/pdb5lac/pdb |
| Descriptor | 3Cl Protease, GLYCEROL (3 entities in total) |
| Functional Keywords | semet derivative, protease, mesonivirus, 3cl, hydrolase |
| Biological source | Cavally virus (CAVV) |
| Total number of polymer chains | 2 |
| Total formula weight | 72097.34 |
| Authors | Kanitz, M.,Heine, A.,Diederich, W.E. (deposition date: 2016-06-14, release date: 2017-07-12, Last modification date: 2024-11-06) |
| Primary citation | Kanitz, M.,Blanck, S.,Heine, A.,Gulyaeva, A.A.,Gorbalenya, A.E.,Ziebuhr, J.,Diederich, W.E. Structural basis for catalysis and substrate specificity of a 3C-like cysteine protease from a mosquito mesonivirus. Virology, 533:21-33, 2019 Cited by PubMed Abstract: Cavally virus (CavV) is a mosquito-borne plus-strand RNA virus in the family Mesoniviridae (order Nidovirales). We present X-ray structures for the CavV 3C-like protease (3CL), as a free enzyme and in complex with a peptide aldehyde inhibitor mimicking the P4-to-P1 residues of a natural substrate. The 3CL structure (refined to 1.94 Å) shows that the protein forms dimers. The monomers are comprised of N-terminal domains I and II, which adopt a chymotrypsin-like fold, and a C-terminal α-helical domain III. The catalytic Cys-His dyad is assisted by a complex network of interactions involving a water molecule that mediates polar contacts between the catalytic His and a conserved Asp located in the domain II-III junction and is suitably positioned to stabilize the developing positive charge of the catalytic His in the transition state during catalysis. The study also reveals the structural basis for the distinct P2 Asn-specific substrate-binding pocket of mesonivirus 3CLs. PubMed: 31078932DOI: 10.1016/j.virol.2019.05.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.94 Å) |
Structure validation
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