2LSN
Solution structure of PFV RNase H domain
Summary for 2LSN
| Entry DOI | 10.2210/pdb2lsn/pdb |
| NMR Information | BMRB: 17745 |
| Descriptor | RNase H (1 entity in total) |
| Functional Keywords | rnase h, viral protein |
| Biological source | Human spumaretrovirus (SFVcpz(hu), Prototype foamy virus) |
| Cellular location | Integrase: Virion (Potential). Protease/Reverse transcriptase/ribonuclease H: Host nucleus (By similarity): P14350 |
| Total number of polymer chains | 1 |
| Total formula weight | 18056.52 |
| Authors | Leo, B.,Schweimer, K.,Woehrl, B. (deposition date: 2012-05-03, release date: 2012-10-17, Last modification date: 2024-05-15) |
| Primary citation | Leo, B.,Schweimer, K.,Rosch, P.,Hartl, M.J.,Wohrl, B.M. The solution structure of the prototype foamy virus RNase H domain indicates an important role of the basic loop in substrate binding. Retrovirology, 9:73-73, 2012 Cited by PubMed Abstract: The ribonuclease H (RNase H) domains of retroviral reverse transcriptases play an essential role in the replication cycle of retroviruses. During reverse transcription of the viral genomic RNA, an RNA/DNA hybrid is created whose RNA strand needs to be hydrolyzed by the RNase H to enable synthesis of the second DNA strand by the DNA polymerase function of the reverse transcriptase. Here, we report the solution structure of the separately purified RNase H domain from prototype foamy virus (PFV) revealing the so-called C-helix and the adjacent basic loop, which both were suggested to be important in substrate binding and activity. PubMed: 22962864DOI: 10.1186/1742-4690-9-73 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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