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Literature summary for 3.1.26.13 extracted from

  • Sarafianos, S.G.; Das, K.; Tantillo, C.; Clark, A.D., Jr.; Ding, J.; Whitcomb, J.M.; Boyer, P.L.; Hughes, S.H.; Arnold, E.
    Crystal structure of HIV-1 reverse transcriptase in complex with a polypurine tract RNA:DNA (2001), EMBO J., 20, 1449-1461.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
purified wild-type enzyme in complex with polypurine tract RNA:DNA oligonucleotide, hanging drop vapour diffusion method, mixing of equal volumes of protein and precipitant solution, the latter contains 100 mM cacodylate, pH 5.6, 29-31% saturated ammonium sulfate, 4°C, X-ray diffraction structure determination and analysis at 3.0 A resolution, molecular replacement Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1 P03366 HIV-1
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Reaction

Reaction Comment Organism Reaction ID
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus. cleavage reaction mechanism and substrate specificity of HIV-1 RNase H, overview Human immunodeficiency virus 1

Synonyms

Synonyms Comment Organism
HIV-1 reverse transcriptase
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Human immunodeficiency virus 1
ribonuclease H
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Human immunodeficiency virus 1
RNase H
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Human immunodeficiency virus 1

General Information

General Information Comment Organism
additional information the polypurine tract, PPT, a purine-rich segment from the HIV-1 genome, is resistant to RNase H cleavage and is used as a primer for second DNA strand synthesis. PPT-enzyme complex structure, detailed overview Human immunodeficiency virus 1
physiological function the enzyme activity and substrate specificity is controlled by the RNase H primer grip, and the width of the minor groove and the trajectroy of the RNA:DNA, both in a sequence-dependent manner Human immunodeficiency virus 1