3QID
Crystal structures and functional analysis of murine norovirus RNA-dependent RNA polymerase
Summary for 3QID
Entry DOI | 10.2210/pdb3qid/pdb |
Related | 1SHO 2B43 3BSO 3H5X |
Descriptor | RNA dependent RNA polymerase, SULFATE ION, MANGANESE (III) ION, ... (5 entities in total) |
Functional Keywords | rna polymerase, viral replication enzyme, transferase |
Biological source | Murine norovirus 1 |
Total number of polymer chains | 3 |
Total formula weight | 179334.14 |
Authors | Kim, K.H.,Intekhab, A.,Lee, J.H. (deposition date: 2011-01-27, release date: 2011-12-21, Last modification date: 2023-11-01) |
Primary citation | Lee, J.H.,Alam, I.,Han, K.R.,Cho, S.,Shin, S.,Kang, S.,Yang, J.M.,Kim, K.H. Crystal structures of murine norovirus-1 RNA-dependent RNA polymerase. J.Gen.Virol., 92:1607-1616, 2011 Cited by PubMed Abstract: Norovirus is one of the leading agents of gastroenteritis and is a major public health concern. In this study, the crystal structures of recombinant RNA-dependent RNA polymerase (RdRp) from murine norovirus-1 (MNV-1) and its complex with 5-fluorouracil (5FU) were determined at 2.5 Å resolution. Crystals with C2 symmetry revealed a dimer with half a dimer in the asymmetrical unit, and the protein exists predominantly as a monomer in solution, in equilibrium with a smaller population of dimers, trimers and hexamers. MNV-1 RdRp exhibited polymerization activity with a right-hand fold typical of polynucleotide polymerases. The metal ion modelled in close proximity to the active site was found to be coordinated tetrahedrally to the carboxyl groups of aspartate clusters. The orientation of 5FU observed in three molecules in the asymmetrical unit was found to be slightly different, but it was stabilized by a network of favourable interactions with the conserved active-site residues Arg185, Asp245, Asp346, Asp347 and Arg395. The information gained on the structural and functional features of MNV-1 RdRp will be helpful in understanding replication of norovirus and in designing novel therapeutic agents against this important pathogen. PubMed: 21471315DOI: 10.1099/vir.0.031104-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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