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