2ITG

CATALYTIC DOMAIN OF HIV-1 INTEGRASE: ORDERED ACTIVE SITE IN THE F185H CONSTRUCT

Summary for 2ITG

• Entry DOI: 10.2210/pdb2itg/pdb
• Descriptor: HUMAN IMMUNODEFICIENCY VIRUS-1 INTEGRASE (2 entities in total)
• Functional Keywords: dna integration, aids, polyprotein, hydrolase, endonuclease, polynucleotidyl transferase, 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: 17921.45

Authors

Bujacz, G.,Alexandratos, J.,Wlodawer, A.,Zhou-Liu, Q.,Clement-Mella, C. (deposition date: 1996-09-13, release date: 1997-03-12, Last modification date: 2024-05-29)

Primary citation

Bujacz, G.,Alexandratos, J.,Qing, Z.L.,Clement-Mella, C.,Wlodawer, A.
The catalytic domain of human immunodeficiency virus integrase: ordered active site in the F185H mutant.
FEBS Lett., 398:175-178, 1996

PubMed Abstract: We solved the structure and traced the complete active site of the catalytic domain of the human immunodeficiency virus type 1 integrase (HIV-1 IN) with the F185H mutation. The only previously available crystal structure, the F185K mutant of this domain, lacks one of the catalytically important residues, E152, located in a stretch of 12 disordered residues [Dyda et al. (1994) Science 266, 1981-1986]. It is clear, however, that the active site of HIV-1 IN observed in either structure cannot correspond to that of the functional enzyme, since the cluster of three conserved carboxylic acids does not create a proper metal-binding site. The conformation of the loop was compared with two different conformations found in the catalytic domain of the related avian sarcoma virus integrase [Bujacz et al. (1995) J. Mol. Biol. 253, 333-346]. Flexibility of the active site region of integrases may be required in order for the enzyme to assume a functional conformation in the presence of substrate and/or cofactors.

PubMed: 8977101
DOI: 10.1016/S0014-5793(96)01236-7

Experimental method

X-RAY DIFFRACTION (2.6 Å)