1ITG

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HIV-1 INTEGRASE: SIMILARITY TO OTHER POLYNUCLEOTIDYL TRANSFERASES

Summary for 1ITG

• Entry DOI: 10.2210/pdb1itg/pdb
• Descriptor: HIV-1 INTEGRASE, CACODYLATE ION (3 entities in total)
• Functional Keywords: dna integration, dna binding (viral)
• Biological source: Human immunodeficiency virus 1
• Cellular location: Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P12497
• Total number of polymer chains: 1
• Total formula weight: 18468.74

Authors

Dyda, F.,Hickman, A.B.,Jenkins, T.M.,Engelman, A.,Craigie, R.,Davies, D.R. (deposition date: 1994-11-21, release date: 1995-05-08, Last modification date: 2024-02-07)

Primary citation

Dyda, F.,Hickman, A.B.,Jenkins, T.M.,Engelman, A.,Craigie, R.,Davies, D.R.
Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases.
Science, 266:1981-1986, 1994

PubMed Abstract: HIV integrase is the enzyme responsible for inserting the viral DNA into the host chromosome; it is essential for HIV replication. The crystal structure of the catalytically active core domain (residues 50 to 212) of HIV-1 integrase was determined at 2.5 A resolution. The central feature of the structure is a five-stranded beta sheet flanked by helical regions. The overall topology reveals that this domain of integrase belongs to a superfamily of polynucleotidyl transferases that includes ribonuclease H and the Holliday junction resolvase RuvC. The active site region is identified by the position of two of the conserved carboxylate residues essential for catalysis, which are located at similar positions in ribonuclease H. In the crystal, two molecules form a dimer with a extensive solvent-inaccessible interface of 1300 A2 per monomer.

PubMed: 7801124

Experimental method

X-RAY DIFFRACTION (2.3 Å)