Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.26.13 extracted from

  • Davies II, J.; Hostomska, Z.; Hostomsky, Z.; Jordan, S.; Matthews, D.
    Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase (1991), Science, 252, 88-95.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of RNase H domain from residue Y427 to L560 as fusion protein in Escherichia coli Human immunodeficiency virus 1

Crystallization (Commentary)

Crystallization (Comment) Organism
isolated recombinant RNase H domain, to 2.4 A resolution. The protein folds into a five-stranded mixed beta sheet flanked by an asymmetric distribution of four alpha helices. Two divalent metal cations bind in the active site surrounded by a cluster of four conserved acidic amino acid residues. The peptide bond cleaved by HIV-1 protease near the polymerase-RNase H junction of polypeptide p66 is completely inaccessible to solvent in the structure reported here, suggesting that the homodimeric p66-p66 precursor of mature RT is asymmetric with one of the two RNase H domains at least partially unfolded Human immunodeficiency virus 1

Metals/Ions

Metals/Ions Comment Organism Structure
additional information in the crystal structure, two divalent metal cations bind in the active site surrounded by a cluster of four conserved acidic amino acid residues Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
-
-
-