1PAF

THE 2.5 ANGSTROMS STRUCTURE OF POKEWEED ANTIVIRAL PROTEIN

1PAF の概要

• エントリーDOI: 10.2210/pdb1paf/pdb
• 分子名称: POKEWEED ANTIVIRAL PROTEIN (2 entities in total)
• 機能のキーワード: protein synthesis inhibitor
• 由来する生物種: Phytolacca americana (American pokeweed)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58682.93

構造登録者

Monzingo, A.F.,Collins, E.J.,Ernst, S.R.,Irvin, J.D.,Robertus, J.D. (登録日: 1992-10-19, 公開日: 1994-01-31, 最終更新日: 2024-10-09)

主引用文献

Monzingo, A.F.,Collins, E.J.,Ernst, S.R.,Irvin, J.D.,Robertus, J.D.
The 2.5 A structure of pokeweed antiviral protein.
J.Mol.Biol., 233:705-715, 1993

PubMed Abstract: 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.

PubMed: 8411176
DOI: 10.1006/jmbi.1993.1547

実験手法

X-RAY DIFFRACTION (2.5 Å)