1dma

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(New page: 200px<br /><applet load="1dma" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dma, resolution 2.5&Aring;" /> '''DOMAIN III OF PSEUDOM...)
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caption="1dma, resolution 2.5&Aring;" />
'''DOMAIN III OF PSEUDOMONAS AERUGINOSA EXOTOXIN COMPLEXED WITH NICOTINAMIDE AND AMP'''<br />
'''DOMAIN III OF PSEUDOMONAS AERUGINOSA EXOTOXIN COMPLEXED WITH NICOTINAMIDE AND AMP'''<br />
==Overview==
==Overview==
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Domain III of Pseudomonas aeruginosa exotoxin A catalyses the transfer of, ADP-ribose from NAD to a modified histidine residue of elongation factor 2, in eukaryotic cells, thus inactivating elongation factor 2. This domain, III is inactive in the intact toxin but is active in the isolated form. We, report here the 2.5-A crystal structure of this isolated domain, crystallized in the presence of NAD and compare it with the corresponding, structure in the intact Pseudomonas aeruginosa exotoxin A. We observe a, significant conformational difference in the active site region from, Arg-458 to Asp-463. Contacts with part of domain II in the intact toxin, prevent the adoption of the isolated domain conformation and provide a, structural explanation for the observed inactivity. Additional electron, density in the active site region corresponds to separate AMP and, nicotinamide and indicates that the NAD has been hydrolyzed. The structure, has been compared with the catalytic domain of the diphtheria toxin, which, was crystallized with ApUp.
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Domain III of Pseudomonas aeruginosa exotoxin A catalyses the transfer of ADP-ribose from NAD to a modified histidine residue of elongation factor 2 in eukaryotic cells, thus inactivating elongation factor 2. This domain III is inactive in the intact toxin but is active in the isolated form. We report here the 2.5-A crystal structure of this isolated domain crystallized in the presence of NAD and compare it with the corresponding structure in the intact Pseudomonas aeruginosa exotoxin A. We observe a significant conformational difference in the active site region from Arg-458 to Asp-463. Contacts with part of domain II in the intact toxin prevent the adoption of the isolated domain conformation and provide a structural explanation for the observed inactivity. Additional electron density in the active site region corresponds to separate AMP and nicotinamide and indicates that the NAD has been hydrolyzed. The structure has been compared with the catalytic domain of the diphtheria toxin, which was crystallized with ApUp.
==About this Structure==
==About this Structure==
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1DMA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with NCA and AMP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DMA OCA].
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1DMA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=NCA:'>NCA</scene> and <scene name='pdbligand=AMP:'>AMP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMA OCA].
==Reference==
==Reference==
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[[Category: adp-ribosylation]]
[[Category: adp-ribosylation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:24:15 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:04 2008''

Revision as of 10:18, 21 February 2008

Image:1dma.gif

1dma, resolution 2.5Å

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DOMAIN III OF PSEUDOMONAS AERUGINOSA EXOTOXIN COMPLEXED WITH NICOTINAMIDE AND AMP

Overview

Domain III of Pseudomonas aeruginosa exotoxin A catalyses the transfer of ADP-ribose from NAD to a modified histidine residue of elongation factor 2 in eukaryotic cells, thus inactivating elongation factor 2. This domain III is inactive in the intact toxin but is active in the isolated form. We report here the 2.5-A crystal structure of this isolated domain crystallized in the presence of NAD and compare it with the corresponding structure in the intact Pseudomonas aeruginosa exotoxin A. We observe a significant conformational difference in the active site region from Arg-458 to Asp-463. Contacts with part of domain II in the intact toxin prevent the adoption of the isolated domain conformation and provide a structural explanation for the observed inactivity. Additional electron density in the active site region corresponds to separate AMP and nicotinamide and indicates that the NAD has been hydrolyzed. The structure has been compared with the catalytic domain of the diphtheria toxin, which was crystallized with ApUp.

About this Structure

1DMA is a Single protein structure of sequence from Pseudomonas aeruginosa with and as ligands. Full crystallographic information is available from OCA.

Reference

The crystal structure of Pseudomonas aeruginosa exotoxin domain III with nicotinamide and AMP: conformational differences with the intact exotoxin., Li M, Dyda F, Benhar I, Pastan I, Davies DR, Proc Natl Acad Sci U S A. 1995 Sep 26;92(20):9308-12. PMID:7568123

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