Reverse transcriptase from Moloney murine leukemia virus (MMLVRT) is an RNA dependent DNA polymerase, which has been used as a fundamental tool for molecular biology and biotechnology. Recent X-ray crystal structure determinations of Moloney murine leukemia virus reverse transcriptase (MoMLV RT) have allowed for more accurate structure/function comparisons to HIV-1 RT than were formerly possible. Previous biochemical studies of MoMLV RT in conjunction with knowledge of sequence homologies to HIV-1 RT and overall fold similarities to RTs in general, provided a foundation upon which to build. Structural and energetic characterization of nucleic acid-binding to the fingers domain of Moloney murine leukemia virus reverse transcriptase. Ein den Menschen infizierender naher Verwandter von Mo-MLV, das Xenotropic Moloney murine leukemia virus-Related Virus , … Epub 2013 Feb 4. Moloney murine leukemia virus reverse transcriptase (MMLVRT) was expressed in silkworm-baculovirus expression vector system. NLM Crystal Structures of an N-terminal Fragment From Moloney Murine Leukemia Virus Reverse Transcriptase Complexed With Nucleic Acid: Functional Implications for Template-Primer Binding to the Fingers Domain J Mol Biol. Dies ist das erste Retrovirus, dessen Genom vollständig sequenziert wurde (1981). 1997;44(2):125-38. doi: 10.1002/(SICI)1097-0282(1997)44:2<125::AID-BIP2>3.0.CO;2-X. Recent X-ray crystal structure determinations of Moloney murine leukemia virus reverse transcriptase (MoMLV RT) have allowed for more accurate structure/function comparisons to HIV-1 RT than were formerly possible. 2017 Nov 17;6(11):2118-2129. doi: 10.1021/acssynbio.7b00150. ScienceDirect ® is a registered trademark of Elsevier B.V. ScienceDirect ® is a registered trademark of Elsevier B.V. Murine leukemia virus reverse transcriptase: Structural comparison with HIV-1 reverse transcriptase. We confirmed that both of the recombinant MMLVRT enzymes have intact DNA polymerase activity.  |  Protein-DNA interactions, which are nearly identical in each of the three lattices, involve four conserved residues in the fingers domain, Asp114, Arg116, Asn119 and Gly191. Get the latest research from NIH: https://www.nih.gov/coronavirus.  |  This fragment includes the fingers and palm domains from Moloney murine leukemia virus reverse transcriptase. Now in the advent of new structural information, more intricate examination of MoMLV RT in its entirety can be realized, and thus the comparisons with HIV-1 RT may be more critically elucidated. Protein-nucleic acid interactions and DNA conformation in a complex of human immunodeficiency virus type 1 reverse transcriptase with a double-stranded DNA template-primer. We have also determined the crystal structure at 3.0 A resolution of the fragment complexed to DNA with a single-stranded template overhang resembling a template-primer substrate. 2017 Jun 29;15(1):54. doi: 10.1186/s12915-017-0387-1. Taken together, these results demonstrate that silkworm-BEVS is a promising alternative strategy to produce the functional and thermostable reverse transcriptase. Structure and functional implications of the polymerase active site region in a complex of HIV-1 RT with a double-stranded DNA template-primer and an antibody Fab fragment at 2.8 A resolution. Synthesis was shown to initiate precisely at the known plus-strand origin. To determine the various roles of RNase H in reverse transcription, we generated a panel of mutations in the RNase H domain of Moloney murine leukemia virus reverse transcriptase based on sequence alignments and the crystal structures of Escherichia coli and human immunodeficiency virus type 1 RNases H (S. W. Blain and S. P. Goff, J. Biol.