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(New page: 200px<br /><applet load="1pag" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pag, resolution 2.8&Aring;" /> '''THE 2.5 ANGSTROMS STR...)
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'''THE 2.5 ANGSTROMS STRUCTURE OF POKEWEED ANTIVIRAL PROTEIN'''<br />
'''THE 2.5 ANGSTROMS STRUCTURE OF POKEWEED ANTIVIRAL PROTEIN'''<br />
==Overview==
==Overview==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PAG OCA].
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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]]
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[[Category: Collins, E.J.]]
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[[Category: Collins, E J.]]
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[[Category: Ernst, S.R.]]
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[[Category: Ernst, S R.]]
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[[Category: Irvin, J.D.]]
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[[Category: Irvin, J D.]]
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[[Category: Monzingo, A.F.]]
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[[Category: Monzingo, A F.]]
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[[Category: Robertus, J.D.]]
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[[Category: Robertus, J D.]]
[[Category: FMP]]
[[Category: FMP]]
[[Category: protein synthesis inhibitor]]
[[Category: protein synthesis inhibitor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:38:13 2007''
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''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


1pag, resolution 2.8Å

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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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