Cloned (Comment) | Organism |
---|---|
recombinant expression of mutant constructs | Human immunodeficiency virus 1 |
Crystallization (Comment) | Organism |
---|---|
crystal structure of domain swapped Rnase H, overview | Human immunodeficiency virus 1 |
Protein Variants | Comment | Organism |
---|---|---|
L429M/E514L | N-terminal truncated constructs include RHDELTANT, corresponding to p66 residues 429-560 with an N-terminal Leu429Met mutation, an extended linker construct, RHDELTANT-EL, in which an additional Pro-Asp-Gln sequence is introduced into RHDELTANT immediately following Gln512, and RHDELTANT(E514L) in which RHDELTANT contains an E514L substitution in the alphaB-alphaD linker | Human immunodeficiency virus 1 |
additional information | effect of N-terminal deletion on monomer-dimer interconversion kinetics, overview. The mutant exhibits large perturbations of the Ile522 and Ile526 resonances corresponding to residues located near the Tyr427 binding pocket, as well as smaller but significant perturbations for several other Ile resonances, consistent with a more subtle, global structural perturbation. As a result of the faster monomer-dimer interconversion rate, even the initial spectrum obtained for the purified dimer sample exhibits significant monomer resonances | Human immunodeficiency virus 1 |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-hydroxyisoquinoline-1,3(2H,4H)-dione | an active site directed inhibitor, stabilizes RH domain helix E | Human immunodeficiency virus 1 |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Human immunodeficiency virus 1 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Human immunodeficiency virus 1 | P04585 | HIV-1 | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | formation of the mature HIV-1 reverse transcriptase (RT) p66/p51 heterodimer requires subunit-specific processing of the p66/p66' homodimer precursor, the ribonuclease H (RH) domain contains an occult cleavage site located near its center. NMR spectroscopic determination of a slow, subunit-specific RH domain unfolding process proposed to result from a residue tug-of-war between the polymerase and RH domains on the functionally inactive, p66' subunit. Structural comparison of the isolated RH domain with a domain swapped RH dimer reveals several intrinsically destabilizing characteristics of the isolated domain that facilitate excursions of Tyr427 from its binding pocket and separation of helices B and D. The enzyme shows a subunit-selective RH domain unfolding pathway in which instability of the Tyr427 binding pocket facilitates its release followed by domain transfer, acting as a trigger for further RH domain destabilization and subsequent unfolding | Human immunodeficiency virus 1 |
Purification (Comment) | Organism |
---|---|
recombinant mutant constructs by gel filtration | Human immunodeficiency virus 1 |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Human immunodeficiency virus 1 |
More | monomer/dimer structural variations of helix B-helix D, overview | Human immunodeficiency virus 1 |
Synonyms | Comment | Organism |
---|---|---|
HIV-1 reverse transcriptase RNase H | - |
Human immunodeficiency virus 1 |
ribonuclease H | - |
Human immunodeficiency virus 1 |
RNaseH | - |
Human immunodeficiency virus 1 |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Human immunodeficiency virus 1 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Human immunodeficiency virus 1 |
General Information | Comment | Organism |
---|---|---|
malfunction | effect of N-terminal deletion on monomer-dimer interconversion kinetics, overview | Human immunodeficiency virus 1 |