1DMA

DOMAIN III OF PSEUDOMONAS AERUGINOSA EXOTOXIN COMPLEXED WITH NICOTINAMIDE AND AMP

Summary for 1DMA

• Entry DOI: 10.2210/pdb1dma/pdb
• Descriptor: EXOTOXIN A, NICOTINAMIDE, ADENOSINE MONOPHOSPHATE, ... (4 entities in total)
• Functional Keywords: adp-ribosylation
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 2
• Total formula weight: 47259.55

Authors

Li, M.,Dyda, F.,Benhar, I.,Pastan, I.,Davies, D. (deposition date: 1995-04-28, release date: 1995-09-15, Last modification date: 2024-02-07)

Primary citation

Li, M.,Dyda, F.,Benhar, I.,Pastan, I.,Davies, D.R.
The crystal structure of Pseudomonas aeruginosa exotoxin domain III with nicotinamide and AMP: conformational differences with the intact exotoxin.
Proc.Natl.Acad.Sci.USA, 92:9308-9312, 1995

PubMed Abstract: 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.

PubMed: 7568123
DOI: 10.1073/pnas.92.20.9308

Experimental method

X-RAY DIFFRACTION (2.5 Å)