1u2r

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(New page: 200px<br /><applet load="1u2r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u2r, resolution 2.6&Aring;" /> '''Crystal Structure of ...)
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[[Image:1u2r.jpg|left|200px]]<br /><applet load="1u2r" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Crystal Structure of ADP-ribosylated Ribosomal Translocase from Saccharomyces cerevisiae'''<br />
'''Crystal Structure of ADP-ribosylated Ribosomal Translocase from Saccharomyces cerevisiae'''<br />
==Overview==
==Overview==
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The crystal structure of ADP-ribosylated yeast elongation factor 2 in the, presence of sordarin and GDP has been determined at 2.6 A resolution. The, diphthamide at the tip of domain IV, which is the target for diphtheria, toxin and Pseudomonas aeruginosa exotoxin A, contains a covalently, attached ADP-ribose that functions as a very potent inhibitor of the, factor. We have obtained an electron density map of ADP-ribosylated, translation factor 2 revealing both the ADP-ribosylation and the, diphthamide. This is the first structure showing the conformation of an, ADP-ribosylated residue and confirms the inversion of configuration at the, glycosidic linkage. Binding experiments show that the ADP-ribosylation has, limited effect on nucleotide binding affinity, on ribosome binding, and on, association with exotoxin A. These results provide insight to the, inhibitory mechanism and suggest that inhibition may be caused by, erroneous interaction of the translation factor with the codon-anticodon, area in the P-site of the ribosome.
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The crystal structure of ADP-ribosylated yeast elongation factor 2 in the presence of sordarin and GDP has been determined at 2.6 A resolution. The diphthamide at the tip of domain IV, which is the target for diphtheria toxin and Pseudomonas aeruginosa exotoxin A, contains a covalently attached ADP-ribose that functions as a very potent inhibitor of the factor. We have obtained an electron density map of ADP-ribosylated translation factor 2 revealing both the ADP-ribosylation and the diphthamide. This is the first structure showing the conformation of an ADP-ribosylated residue and confirms the inversion of configuration at the glycosidic linkage. Binding experiments show that the ADP-ribosylation has limited effect on nucleotide binding affinity, on ribosome binding, and on association with exotoxin A. These results provide insight to the inhibitory mechanism and suggest that inhibition may be caused by erroneous interaction of the translation factor with the codon-anticodon area in the P-site of the ribosome.
==About this Structure==
==About this Structure==
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1U2R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MG, APR, SO1 and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U2R OCA].
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1U2R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=APR:'>APR</scene>, <scene name='pdbligand=SO1:'>SO1</scene> and <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2R OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Andersen, G.R.]]
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[[Category: Andersen, G R.]]
[[Category: Jorgensen, R.]]
[[Category: Jorgensen, R.]]
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[[Category: Merrill, A.R.]]
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[[Category: Merrill, A R.]]
[[Category: Nilsson, J.]]
[[Category: Nilsson, J.]]
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[[Category: Prentice, G.A.]]
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[[Category: Prentice, G A.]]
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[[Category: Teal, D.J.]]
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[[Category: Teal, D J.]]
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[[Category: Yates, S.P.]]
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[[Category: Yates, S P.]]
[[Category: APR]]
[[Category: APR]]
[[Category: GDP]]
[[Category: GDP]]
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[[Category: sordarin]]
[[Category: sordarin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:20:02 2008''

Revision as of 13:20, 21 February 2008


1u2r, resolution 2.6Å

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Crystal Structure of ADP-ribosylated Ribosomal Translocase from Saccharomyces cerevisiae

Overview

The crystal structure of ADP-ribosylated yeast elongation factor 2 in the presence of sordarin and GDP has been determined at 2.6 A resolution. The diphthamide at the tip of domain IV, which is the target for diphtheria toxin and Pseudomonas aeruginosa exotoxin A, contains a covalently attached ADP-ribose that functions as a very potent inhibitor of the factor. We have obtained an electron density map of ADP-ribosylated translation factor 2 revealing both the ADP-ribosylation and the diphthamide. This is the first structure showing the conformation of an ADP-ribosylated residue and confirms the inversion of configuration at the glycosidic linkage. Binding experiments show that the ADP-ribosylation has limited effect on nucleotide binding affinity, on ribosome binding, and on association with exotoxin A. These results provide insight to the inhibitory mechanism and suggest that inhibition may be caused by erroneous interaction of the translation factor with the codon-anticodon area in the P-site of the ribosome.

About this Structure

1U2R is a Single protein structure of sequence from Saccharomyces cerevisiae with , , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of ADP-ribosylated ribosomal translocase from Saccharomyces cerevisiae., Jorgensen R, Yates SP, Teal DJ, Nilsson J, Prentice GA, Merrill AR, Andersen GR, J Biol Chem. 2004 Oct 29;279(44):45919-25. Epub 2004 Aug 16. PMID:15316019

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