1pag
From Proteopedia
(New page: 200px<br /><applet load="1pag" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pag, resolution 2.8Å" /> '''THE 2.5 ANGSTROMS STR...) |
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caption="1pag, resolution 2.8Å" /> | caption="1pag, resolution 2.8Å" /> | ||
'''THE 2.5 ANGSTROMS STRUCTURE OF POKEWEED ANTIVIRAL PROTEIN'''<br /> | '''THE 2.5 ANGSTROMS STRUCTURE OF POKEWEED ANTIVIRAL PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
- | The pokeweed antiviral protein (PAP), isolated from the leaves of | + | 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== | ==About this Structure== | ||
- | 1PAG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phytolacca_americana Phytolacca americana] with FMP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1PAG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phytolacca_americana Phytolacca americana] with <scene name='pdbligand=FMP:'>FMP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PAG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Phytolacca americana]] | [[Category: Phytolacca americana]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
- | [[Category: Collins, E | + | [[Category: Collins, E J.]] |
- | [[Category: Ernst, S | + | [[Category: Ernst, S R.]] |
- | [[Category: Irvin, J | + | [[Category: Irvin, J D.]] |
- | [[Category: Monzingo, A | + | [[Category: Monzingo, A F.]] |
- | [[Category: Robertus, J | + | [[Category: Robertus, J D.]] |
[[Category: FMP]] | [[Category: FMP]] | ||
[[Category: protein synthesis inhibitor]] | [[Category: protein synthesis inhibitor]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:59 2008'' |
Revision as of 12:27, 21 February 2008
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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 with as ligand. 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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