1aaf

Solution NMR

NUCLEOCAPSID ZINC FINGERS DETECTED IN RETROVIRUSES: EXAFS STUDIES ON INTACT VIRUSES AND THE SOLUTION-STATE STRUCTURE OF THE NUCLEOCAPSID PROTEIN FROM HIV-1

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-138839 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nucleocapsid protein p7 Chain: A
Molecule details ›
Chain: A
Length: 55 amino acids
Theoretical weight: 6.47 KDa
Source organism: HIV-1 M:B_MN
Expression system: Escherichia coli
UniProt:
  • Canonical: P05961 (Residues: 381-435; Coverage: 4%)
Gene name: gag-pol
Sequence domains: Zinc knuckle
Structure domains: Zinc finger, CCHC-type

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli