1DMA

DOMAIN III OF PSEUDOMONAS AERUGINOSA EXOTOXIN COMPLEXED WITH NICOTINAMIDE AND AMP

1DMA の概要

• エントリーDOI: 10.2210/pdb1dma/pdb
• 分子名称: EXOTOXIN A, NICOTINAMIDE, ADENOSINE MONOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: adp-ribosylation
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47259.55

構造登録者

Li, M.,Dyda, F.,Benhar, I.,Pastan, I.,Davies, D. (登録日: 1995-04-28, 公開日: 1995-09-15, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)