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 | UniProt | Comment | Textmining |
---|---|---|---|
Human immunodeficiency virus 1 | P03366 | HIV-1 | - |
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 | Comment | Organism |
---|---|---|
HIV-1 reverse transcriptase | - |
Human immunodeficiency virus 1 |
ribonuclease H | - |
Human immunodeficiency virus 1 |
RNase H | - |
Human immunodeficiency virus 1 |
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 |