1pag

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|PDB= 1pag |SIZE=350|CAPTION= <scene name='initialview01'>1pag</scene>, resolution 2.8&Aring;
|PDB= 1pag |SIZE=350|CAPTION= <scene name='initialview01'>1pag</scene>, resolution 2.8&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=FMP:FORMYCIN-5'-MONOPHOSPHATE'>FMP</scene>
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|LIGAND= <scene name='pdbligand=FMP:FORMYCIN-5&#39;-MONOPHOSPHATE'>FMP</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
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[[Category: protein synthesis inhibitor]]
[[Category: protein synthesis inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:22:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:11:11 2008''

Revision as of 11:11, 23 March 2008

Image:1pag.jpg


PDB ID 1pag

Drag the structure with the mouse to rotate
, resolution 2.8Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



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

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