Literature summary for 3.1.26.13 extracted from

Zheng, X.; Pedersen, L.C.; Gabel, S.A.; Mueller, G.A.; DeRose, E.F.; London, R.E.
Unfolding the HIV-1 reverse transcriptase RNase H domain - how to lose a molecular tug-of-war (2016), Nucleic Acids Res., 44, 1776-1788 .

Search for more literature for 3.1.26.13

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of mutant constructs	Human immunodeficiency virus 1

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of domain swapped Rnase H, overview	Human immunodeficiency virus 1

Protein Variants

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

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

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Human immunodeficiency virus 1

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	P04585	HIV-1	-

Posttranslational Modification

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 (Commentary)

Purification (Comment)	Organism
recombinant mutant constructs by gel filtration	Human immunodeficiency virus 1

Subunits

Subunits	Comment	Organism
dimer	-	Human immunodeficiency virus 1
More	monomer/dimer structural variations of helix B-helix D, overview	Human immunodeficiency virus 1

Synonyms

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 [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Human immunodeficiency virus 1

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Human immunodeficiency virus 1

General Information

General Information	Comment	Organism
malfunction	effect of N-terminal deletion on monomer-dimer interconversion kinetics, overview	Human immunodeficiency virus 1

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Release 2023.1 (January 2023)