1HHP

THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTYL PROTEASE FROM THE HIV-1 ISOLATE BRU

Summary for 1HHP

• Entry DOI: 10.2210/pdb1hhp/pdb
• Descriptor: UNLIGANDED HIV-1 PROTEASE (1 entity in total)
• Functional Keywords: hydrolase(acid proteinase)
• Biological source: Human immunodeficiency virus type 1 (BRU ISOLATE)
• 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): P03367
• Total number of polymer chains: 1
• Total formula weight: 10803.76

Authors

Spinelli, S.,Alzari, P.M. (deposition date: 1992-05-27, release date: 1992-10-15, Last modification date: 2024-02-07)

Primary citation

Spinelli, S.,Liu, Q.Z.,Alzari, P.M.,Hirel, P.H.,Poljak, R.J.
The three-dimensional structure of the aspartyl protease from the HIV-1 isolate BRU.
Biochimie, 73:1391-1396, 1991

PubMed Abstract: The crystal structure of the aspartyl protease encoded by the gene pol of the human immunodeficiency virus (HIV-1, isolate BRU) has been determined to 2.7 A resolution. The enzyme, expressed as an insoluble denatured polypeptide in inclusion bodies of Escherichia coli has been renatured and crystallized. It differs by several amino acid replacements from the homologous enzymes of other HIV-1 isolates. A superposition of the C alpha-backbone of the BRU protease with that of the SF2 protease gives a roots mean square positional difference of 0.45 A. Thus, neither the denaturation/renaturation process nor the amino acid replacements have a noticeable effect on the three-dimensional structure of the BRU protease or on the detailed conformation of the catalytic site, which is very similar to that of other aspartyl proteases.

PubMed: 1799632
DOI: 10.1016/0300-9084(91)90169-2

Experimental method

X-RAY DIFFRACTION (2.7 Å)