1baj

X-ray diffraction
2.6Å resolution

HIV-1 CAPSID PROTEIN C-TERMINAL FRAGMENT PLUS GAG P2 DOMAIN

Released:
Primary publication:
Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution.
Acta Crystallogr D Biol Crystallogr 55 85-92 (1999)
PMID: 10089398

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146209 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Capsid protein p24 Chain: A
Molecule details ›
Chain: A
Length: 101 amino acids
Theoretical weight: 11.11 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P12497 (Residues: 277-377; Coverage: 7%)
Gene name: gag-pol
Sequence domains: Gag protein p24 C-terminal domain
Structure domains: Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein; Chain A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: I41
Unit cell:
a: 61.33Å b: 61.33Å c: 59.57Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.207 0.275
Expression system: Escherichia coli BL21(DE3)