Download MendeleyX-ray crystallographic analysis of the structural basis for the interaction of pokeweed antiviral protein with guanine residues of ribosomal RNA.
Kurinov, I.V., Rajamohan, F., Venkatachalam, T.K., Uckun, F.M.(1999) Protein Sci 8: 2399-2405
- PubMed: 10595542
- DOI: https://doi.org/10.1110/ps.8.11.2399
- Primary Citation of Related Structures:
1D6A - PubMed Abstract:
Pokeweed antiviral protein (PAP) is a ribosome-inactivating protein (RIP), which enzymatically removes a single adenine base from a conserved, surface exposed loop sequence of ribosomal rRNA. We now present unprecedented experimental evidence that PAP can release not only adenine but guanine as well from Escherichia coli rRNA, albeit at a rate 20 times slower than for adenine. We also report X-ray structure analysis and supporting modeling studies for the interactions of PAP with guanine. Our modeling studies indicated that PAP can accommodate a guanine base in the active site pocket without large conformational changes. This prediction was experimentally confirmed, since a guanine base was visible in the active site pocket of the crystal structure of the PAP-guanine complex.
Organizational Affiliation:
Department of Structural Biology, Hughes Institute, Roseville, Minnesota 55113, USA. igor@ih.org
