Science. 1994 Dec 23;266(5193):1981-6.

Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases.

Dyda F, Hickman AB, Jenkins TM, Engelman A, Craigie R, Davies DR.

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Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD 20892-0560.

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.

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Science. 1994 Dec 23;266(5193):1946.

PMID:: 7801124; [PubMed - indexed for MEDLINE]

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Structures reported by this article

Crystal Structure Of The Catalytic Domain Of Hiv-1 Integrase: Similarity To Other Polynucleotidyl Transferases

PDB: 1ITG

Source: Human immunodeficiency virus 1

Method: X-Ray Diffraction

Resolution: 2.3 Å

See all 8 structures...

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Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases.

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