Structural highlights
Function
[RIP1_PHYAM] Inhibits viral infection of plants, and protein synthesis in vitro.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The pokeweed antiviral protein (PAP), isolated from the leaves of Phytolacca americana, is one of a family of plant and bacterial ribosome-inhibiting proteins (RIPs) which act as specific N-glycosidases on rRNA. Here we report the three-dimensional structure of PAP determined to 2.5 A resolution by X-ray crystallography. After 14 rounds of refinement, the R factor is 0.17 for 5.0 to 2.5 A data. The protein is homologous with the A chain of ricin and exhibits a very similar folding pattern. The positions of key active site residues are also similar. We also report the 2.8 A structure of PAP complexed with a substrate analog, formycin 5'-monophosphate. As seen previously in ricin, the formycin ring is stacked between invariant tyrosines 72 and 123. Arg179 bonds to N-3 which is thought to be important in catalysis.
The 2.5 A structure of pokeweed antiviral protein.,Monzingo AF, Collins EJ, Ernst SR, Irvin JD, Robertus JD J Mol Biol. 1993 Oct 20;233(4):705-15. PMID:8411176[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Monzingo AF, Collins EJ, Ernst SR, Irvin JD, Robertus JD. The 2.5 A structure of pokeweed antiviral protein. J Mol Biol. 1993 Oct 20;233(4):705-15. PMID:8411176 doi:http://dx.doi.org/10.1006/jmbi.1993.1547
