PDBe 1tam

Solution NMR

HUMAN IMMUNODEFICIENCY VIRUS, NMR, MINIMIZED AVERAGE STRUCTURE

Released:
Source organism: HIV-1 M:B_HXB2R
Primary publication:
Refined solution structure of p17, the HIV matrix protein.
Biochem. Soc. Trans. 23 725-9 (1995)
PMID: 8654825

Function and Biology Details

Reactions catalysed:
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. 
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). 
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro. 
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid. 
Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Matrix protein p17 Chain: A
Molecule details ›
Chain: A
Length: 132 amino acids
Theoretical weight: 14.91 KDa
Source organism: HIV-1 M:B_HXB2R
Expression system: Escherichia coli
UniProt:
  • Canonical: P04585 (Residues: 1-132; Coverage: 9%)
Gene name: gag-pol
Sequence domains: gag gene protein p17 (matrix protein)
Structure domains: DNA polymerase; domain 1

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli