2CJQ
Bovine viral diarrhea virus CP7-R12 RNA-dependent RNA polymerase
Summary for 2CJQ
| Entry DOI | 10.2210/pdb2cjq/pdb |
| Related | 2AJJ 2AJM 2AJN 2AJO |
| Descriptor | RNA-DIRECTED RNA POLYMERASE (2 entities in total) |
| Functional Keywords | transferase, rna-dependent rna polymerase, nucleotidyltransferase, bovine viral diarrhea virus, bvdv, helicase, membrane, protease, hydrolase, rna-directed rna polymerase, viral polymerase, nucleotide-binding, transmembrane, thiol protease, serine protease, atp-binding, polyprotein, glycoprotein |
| Biological source | BOVINE VIRAL DIARRHEA VIRUS (BVDV) |
| Cellular location | E(rns) glycoprotein: Host membrane; Peripheral membrane protein. Envelope glycoprotein E2: Host cell surface (By similarity). Cysteine protease NS2: Host membrane; Multi- pass membrane protein (Potential): Q96662 |
| Total number of polymer chains | 1 |
| Total formula weight | 82302.22 |
| Authors | Choi, K.H.,Gallei, A.,Becher, P.,Rossmann, M.G. (deposition date: 2006-04-05, release date: 2006-07-19, Last modification date: 2023-12-13) |
| Primary citation | Choi, K.H.,Gallei, A.,Becher, P.,Rossmann, M.G. The Structure of Bovine Viral Diarrhea Virus RNA-Dependent RNA Polymerase and its Amino-Terminal Domain. Structure, 14:1107-, 2006 Cited by PubMed Abstract: Viral RNA-dependent RNA polymerases (RdRp) differ from DNA-dependent RNA polymerases, DNA-dependent DNA polymerases, and reverse transcriptases in that RdRps contain "fingertips" consisting of several polypeptide strands in the fingers domain interacting with the thumb domain. The crystal structure of bovine viral diarrhea virus (BVDV) RdRp containing an Asn438 duplication shows that the "N-terminal domain," which occurs only in pestiviruses such as BVDV, interacts with the polymerase component of the same polypeptide chain. This contrasts with the domain swapping observed in the previously determined structure of the BVDV NADL strain RdRp. By comparison with the NADL structure and through the use of biochemical data, it is possible that the N-terminal domain, in conjunction with the fingertips, is required to bind and assist the translocation of the RNA template. The partial disorder of the loop containing the additional Asn438 residue may explain the low replication rate of the recombinant compared with the wild-type virus. PubMed: 16843892DOI: 10.1016/J.STR.2006.05.020 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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