1VSF

ASV INTEGRASE CORE DOMAIN WITH MN(II) COFACTOR AND HEPES LIGAND, HIGH MG CONCENTRATION FORM

Summary for 1VSF

• Entry DOI: 10.2210/pdb1vsf/pdb
• Descriptor: INTEGRASE, MANGANESE (II) ION, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: hydrolase, endonuclease, endoribonuclease
• Biological source: Rous sarcoma virus (strain Schmidt-Ruppin)
• Cellular location: Matrix protein p19: Virion (Potential). Capsid protein p27: Virion (Potential). Nucleocapsid protein p12: Virion (Potential): P03354
• Total number of polymer chains: 1
• Total formula weight: 17016.47

Authors

Bujacz, G.,Jaskolski, M.,Alexandratos, J.,Wlodawer, A. (deposition date: 1995-11-29, release date: 1996-04-03, Last modification date: 2024-02-14)

Primary citation

Bujacz, G.,Jaskolski, M.,Alexandratos, J.,Wlodawer, A.,Merkel, G.,Katz, R.A.,Skalka, A.M.
The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations.
Structure, 4:89-96, 1996

PubMed Abstract: Members of the structurally-related superfamily of enzymes that includes RNase H, RuvC resolvase, MuA transposase, and retroviral integrase require divalent cations for enzymatic activity. So far, cation positions are reported in the X-ray crystal structures of only two of these proteins, E. coli and human immunodeficiency virus 1 (HIV-1) RNase H. Details of the placement of metal ions in the active site of retroviral integrases are necessary for the understanding of the catalytic mechanism of these enzymes.

PubMed: 8805516
DOI: 10.1016/S0969-2126(96)00012-3

Experimental method

X-RAY DIFFRACTION (2.05 Å)