1HHS
RNA dependent RNA polymerase from dsRNA bacteriophage phi6
Summary for 1HHS
| Entry DOI | 10.2210/pdb1hhs/pdb |
| Related | 1HHT 1HI0 1HI1 1HI8 |
| Descriptor | RNA-DIRECTED RNA POLYMERASE, MANGANESE (II) ION (3 entities in total) |
| Functional Keywords | rna polymerase, viral polymerase, transferase |
| Biological source | BACTERIOPHAGE PHI-6 (PHAGE PHI 6) |
| Cellular location | Virion: P11124 |
| Total number of polymer chains | 3 |
| Total formula weight | 224874.42 |
| Authors | Grimes, J.M.,Butcher, S.J.,Makeyev, E.V.,Bamford, D.H.,Stuart, D.I. (deposition date: 2000-12-28, release date: 2001-03-27, Last modification date: 2024-05-08) |
| Primary citation | Butcher, S.J.,Grimes, J.M.,Makeyev, E.V.,Bamford, D.H.,Stuart, D.I. A Mechanism for Initiating RNA-Dependent RNA Polymerization Nature, 410:235-, 2001 Cited by PubMed Abstract: In most RNA viruses, genome replication and transcription are catalysed by a viral RNA-dependent RNA polymerase. Double-stranded RNA viruses perform these operations in a capsid (the polymerase complex), using an enzyme that can read both single- and double-stranded RNA. Structures have been solved for such viral capsids, but they do not resolve the polymerase subunits in any detail. Here we show that the 2 A resolution X-ray structure of the active polymerase subunit from the double-stranded RNA bacteriophage straight phi6 is highly similar to that of the polymerase of hepatitis C virus, providing an evolutionary link between double-stranded RNA viruses and flaviviruses. By crystal soaking and co-crystallization, we determined a number of other structures, including complexes with oligonucleotide and/or nucleoside triphosphates (NTPs), that suggest a mechanism by which the incoming double-stranded RNA is opened up to feed the template through to the active site, while the substrates enter by another route. The template strand initially overshoots, locking into a specificity pocket, and then, in the presence of cognate NTPs, reverses to form the initiation complex; this process engages two NTPs, one of which acts with the carboxy-terminal domain of the protein to prime the reaction. Our results provide a working model for the initiation of replication and transcription. PubMed: 11242087DOI: 10.1038/35065653 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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