5DMQ

Crystal structure of mouse eRF1 in complex with Reverse Transcriptase (RT) of Moloney Murine Leukemia Virus

Summary for 5DMQ

• Entry DOI: 10.2210/pdb5dmq/pdb
• Related: 5DMR
• Descriptor: Reverse transcriptase/ribonuclease H p80, Eukaryotic peptide chain release factor subunit 1 (2 entities in total)
• Functional Keywords: complex, erf1, rt, transferase, hydrolase-translation complex, hydrolase/translation
• Biological source: Moloney murine leukemia virus (isolate Shinnick) (MoMLV); More
• Cellular location: Gag-Pol polyprotein: Host cell membrane ; Lipid-anchor . Matrix protein p15: Virion . Capsid protein p30: Virion . Nucleocapsid protein p10: Virion : P03355; Cytoplasm : Q8BWY3
• Total number of polymer chains: 2
• Total formula weight: 121236.80

Authors

Tang, T.,Song, H. (deposition date: 2015-09-09, release date: 2016-07-06, Last modification date: 2024-03-20)

Primary citation

Tang, X.,Zhu, Y.,Baker, S.L.,Bowler, M.W.,Chen, B.J.,Chen, C.,Hogg, J.R.,Goff, S.P.,Song, H.
Structural basis of suppression of host translation termination by Moloney Murine Leukemia Virus
Nat Commun, 7:12070-12070, 2016

PubMed Abstract: Retroviral reverse transcriptase (RT) of Moloney murine leukemia virus (MoMLV) is expressed in the form of a large Gag-Pol precursor protein by suppression of translational termination in which the maximal efficiency of stop codon read-through depends on the interaction between MoMLV RT and peptidyl release factor 1 (eRF1). Here, we report the crystal structure of MoMLV RT in complex with eRF1. The MoMLV RT interacts with the C-terminal domain of eRF1 via its RNase H domain to sterically occlude the binding of peptidyl release factor 3 (eRF3) to eRF1. Promotion of read-through by MoMLV RNase H prevents nonsense-mediated mRNA decay (NMD) of mRNAs. Comparison of our structure with that of HIV RT explains why HIV RT cannot interact with eRF1. Our results provide a mechanistic view of how MoMLV manipulates the host translation termination machinery for the synthesis of its own proteins.

PubMed: 27329342
DOI: 10.1038/ncomms12070

Experimental method

X-RAY DIFFRACTION (4 Å)