1vsi
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ASV INTEGRASE CORE DOMAIN WITH CA(II) COFACTOR
OverviewOverview
Retroviral integrases (INs) contain two known metal binding domains. The, N-terminal domain includes a zinc finger motif and has been shown to bind, Zn2+, whereas the central catalytic core domain includes a triad of acidic, amino acids that bind Mn2+ or Mg2+, the metal cofactors required for, enzymatic activity. The integration reaction occurs in two distinct steps;, the first is a specific endonucleolytic cleavage step called "processing,", and the second is a polynucleotide transfer or "joining" step. Our, previous results showed that the metal preference for in vitro activity of, avian sarcoma virus IN is Mn2+ > Mg2+ and that a single cation of either, metal is coordinated by two of the three critical active site residues, (Asp-64 and Asp-121) in crystals of the isolated catalytic ... [(full description)]
About this StructureAbout this Structure
1VSI is a [Single protein] structure of sequence from [Rous sarcoma virus] with CA and EPE as [ligands]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
ReferenceReference
Binding of different divalent cations to the active site of avian sarcoma virus integrase and their effects on enzymatic activity., Bujacz G, Alexandratos J, Wlodawer A, Merkel G, Andrake M, Katz RA, Skalka AM, J Biol Chem. 1997 Jul 18;272(29):18161-8. PMID:9218451
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