1MFY
SOLUTION STRUCTURE OF INFLUENZA A VIRUS C4 PROMOTER
Summary for 1MFY
| Entry DOI | 10.2210/pdb1mfy/pdb |
| Related | 1M82 |
| NMR Information | BMRB: 5553 |
| Descriptor | C4 promoter of influneza A virus (1 entity in total) |
| Functional Keywords | influenza a virus promoter, internal loop, single adenine bulge, c4, natural variant, rna |
| Total number of polymer chains | 1 |
| Total formula weight | 9911.91 |
| Authors | Lee, M.-K.,Bae, S.-H.,Park, C.-J.,Cheong, H.-K.,Cheong, C.,Choi, B.-S. (deposition date: 2002-08-14, release date: 2002-09-18, Last modification date: 2024-05-22) |
| Primary citation | Lee, M.-K.,Bae, S.-H.,Park, C.-J.,Cheong, H.-K.,Cheong, C.,Choi, B.-S. A single-nucleotide natural variation (U4 to C4) in an influenza A virus promoter exhibits a large structural change: implications for differential viral RNA synthesis by RNA-dependent RNA polymerase. Nucleic Acids Res., 31:1216-1223, 2003 Cited by PubMed Abstract: The influenza A virus promoter is recognized by the influenza A virus RNA-dependent RNA polymerase, and directs both transcription and replication of the viral RNA genome. Within the sequence of this promoter, flu strains exhibit a natural, unique variation, either a U or a C, at the fourth position from the 3' end. Promoters that contain a C residue (C4 promoter), which are invariably found in genome segments that encode the three RNA polymerase subunits (PB1, PB2 and PA), down-regulate transcription but activate genome replication. Here, we have determined the structure of the C4 promoter by NMR spectroscopy and compared it with the structure of the U4 promoter, which was determined previously. The structure of the internal loop in the C4 promoter is similar to that of the U4 promoter. However, the terminal stem of the C4 promoter is strikingly different from that of the U4 promoter. These structural data suggest that the internal loop is important for polymerase binding to the promoter, and the terminal stem is crucial for differential regulation of transcription and replication. PubMed: 12582241DOI: 10.1093/nar/gkg214 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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