4MH8

The crystal structure of the monomeric reverse transcriptase from moloney murine leukemia virus

Replaces:  1RW3

Summary for 4MH8

• Entry DOI: 10.2210/pdb4mh8/pdb
• Related: 1rw3
• Descriptor: Reverse transcriptase/ribonuclease H p80 (1 entity in total)
• Functional Keywords: rna and dna dependent dna polymerase, reverse transcriptase, transferase, replication, hydrolase
• Biological source: Moloney murine leukemia virus (MoMLV)
• Total number of polymer chains: 1
• Total formula weight: 72573.55

Authors

Das, D.,Georgiadis, M.M. (deposition date: 2013-08-29, release date: 2013-10-16, Last modification date: 2023-09-20)

Primary citation

Das, D.,Georgiadis, M.M.
The crystal structure of the monomeric reverse transcriptase from Moloney murine leukemia virus.
Structure, 12:819-829, 2004

PubMed Abstract: Reverse 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.

PubMed: 15130474
DOI: 10.1016/j.str.2004.02.032

Experimental method

X-RAY DIFFRACTION (3 Å)