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The crystal structure of the monomeric reverse transcriptase from moloney murine leukemia virusThe crystal structure of the monomeric reverse transcriptase from moloney murine leukemia virus
Structural highlights
Publication Abstract from PubMedReverse transcriptases (RTs) are multidomain enzymes of variable architecture that couple both RNA- and DNA-directed DNA polymerase activities with an RNase H activity specific for an RNA:DNA hybrid in order to replicate the single-stranded RNA genome of the retrovirus. Previous structural work has been reported for the heterodimeric HIV-1 and HIV-2 RTs. We now report the first crystal structure of the full-length Moloney murine leukemia virus (MMLV) RT at 3.0 A resolution. The structure reveals a clamp-shaped molecule resulting from the relative positions of the thumb, connection, and RNase H domains that is strikingly different from the HIV-1 RT and provides the first example of a monomeric reverse transcriptase. A comparative analysis with related DNA polymerases suggests a unique trajectory for the template-primer exiting the polymerase active site and provides insights regarding processive DNA synthesis by MMLV RT. The crystal structure of the monomeric reverse transcriptase from Moloney murine leukemia virus.,Das D, Georgiadis MM Structure. 2004 May;12(5):819-29. PMID:15130474[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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