1dma

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spinqualitylabelsall models 1dma, resolution 2.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 NCA and AMP 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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