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2.4.2.36: NAD+-diphthamide ADP-ribosyltransferase

This is an abbreviated version!
For detailed information about NAD+-diphthamide ADP-ribosyltransferase, go to the full flat file.

Word Map on EC 2.4.2.36

Reaction

NAD+
+
diphthamide-[translation elongation factor 2]
=
nicotinamide
 +
N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]

Synonyms

(adenosine diphosphoribose)transferase, nicotinamide adenine dinucleotide-elongation factor 2, ADP-ribosyltransferase, cholera toxin, cholix, cholix toxin, chxA, CTB, diphthamide-specific ADPRT, diphthamide-specific mono-ADP-ribosylating toxin, EHI 155600, EhToxin-l, EhToxin-like, ExoA, ExoA(c), exotoxin A, mono(ADPribosyl)transferase, mono-ADP-ribosyltransferase, NAD(+)-diphthamide ADP-ribosyltransferase, NAD-diphthamide ADP-ribosyltransferase, NAD-diphthamide ADP-ribosyltransferase NAD-elongation factor 2 ADP-ribosyltransferase, NAD:elongation factor 2-adenosine diphosphate ribose-transferase

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.36 NAD+-diphthamide ADP-ribosyltransferase

Crystallization

Crystallization on EC 2.4.2.36 - NAD+-diphthamide ADP-ribosyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 12% (w/v) polyethylene glycol 6000, 0.1 M MES pH 5.5, 0.1 M ammonium acetate
in complex with NAD+ and eEF2, PDB: 3B8H (mutant E546A), 3B82 (mutant E546H), 3B78 (mutant R551H), 2ZIT (wild-type), specific interactions of active-site loop1 with NAD+ and diphthamide results in solvent cover for dinucleotide-binding pocket and coordinates and stabilizes NAD+ in the active-site cleft during ADPRT reaction (transition-state model), crystals are of space group P(1)2(1), C2 symmetry, unit cell parameters: a: 326.9-329.4, b: 68.1-69.2, c: 190.0-191.6, beta: 102.9-103.3°, precipitant: PEG-8K or PEG-10K, 6-8%, 1.25 mM NAD+ (in cryo-protection buffer, pH 6.0) soaked into crystals
a 1.8 A crystal structure of cholix in complex with its natural substrate, nicotinamide adenine dinucleotide
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