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'''THE 2.5 ANGSTROMS STRUCTURE OF POKEWEED ANTIVIRAL PROTEIN''' | '''THE 2.5 ANGSTROMS STRUCTURE OF POKEWEED ANTIVIRAL PROTEIN''' | ||
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[[Category: Monzingo, A F.]] | [[Category: Monzingo, A F.]] | ||
[[Category: Robertus, J D.]] | [[Category: Robertus, J D.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:52:53 2008'' | |
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Revision as of 01:52, 3 May 2008
THE 2.5 ANGSTROMS STRUCTURE OF POKEWEED ANTIVIRAL PROTEIN
Overview
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.
About this Structure
1PAG is a Single protein structure of sequence from Phytolacca americana. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 04:52:53 2008
