1WQS
Crystal structure of Norovirus 3C-like protease
Summary for 1WQS
| Entry DOI | 10.2210/pdb1wqs/pdb |
| Descriptor | 3C-like protease, MERCURY (II) ION, L(+)-TARTARIC ACID, ... (5 entities in total) |
| Functional Keywords | norovirus, 3c-like protease, chymotrypsin like protease, oxyanion hole, norwalk-like virus, hydrolase |
| Biological source | Chiba virus |
| Total number of polymer chains | 4 |
| Total formula weight | 76226.96 |
| Authors | Nakamura, K.,Someya, Y.,Kumasaka, T.,Tanaka, N. (deposition date: 2004-10-01, release date: 2005-10-04, Last modification date: 2024-12-25) |
| Primary citation | Nakamura, K.,Someya, Y.,Kumasaka, T.,Ueno, G.,Yamamoto, M.,Sato, T.,Takeda, N.,Miyamura, T.,Tanaka, N. A norovirus protease structure provides insights into active and substrate binding site integrity J.Virol., 79:13685-13693, 2005 Cited by PubMed Abstract: Norovirus 3C-like proteases are crucial to proteolytic processing of norovirus polyproteins. We determined the crystal structure of the 3C-like protease from Chiba virus, a norovirus, at 2.8-A resolution. An active site including Cys139 and His30 is present, as is a hydrogen bond network that stabilizes the active site conformation. In the oxyanion hole backbone, a structural difference was observed probably upon substrate binding. A peptide substrate/enzyme model shows that several interactions between the two components are critical for substrate binding and that the S1 and S2 sites appropriately accommodate the substrate P1 and P2 residues, respectively. Knowledge of the structure and a previous mutagenesis study allow us to correlate proteolysis and structure. PubMed: 16227288DOI: 10.1128/JVI.79.21.13685-13693.2005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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