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2.4.2.31: NAD+-protein-arginine ADP-ribosyltransferase

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

Word Map on EC 2.4.2.31

Reaction

NAD+
+
L-arginine
=
nicotinamide
 +
Nomega-(ADP-D-ribosyl)-L-arginine
 +
H+

Synonyms

(adenosine diphosphoribose)transferase, nicotinamide adenine dinucleotide-arginine, actin-specific ADP-ribosyltransferase, ADP-ribosyl-acceptor hydrolase 1, ADP-ribosyltransferase, ADP-ribosyltransferase enzymatic component, ADP-ribosyltransferase-2, ADPRT, alloantigen Rt6.1 , alloantigen Rt6.2 , ALT, arginine ADP-ribosyltransferase 1, arginine specific ADP-ribosyltransferase, arginine specific mono-ADP-ribosyltransferase, arginine-specific adenosine diphosphate ribosyltransferase 1, arginine-specific ADP-ribosyltransferase, arginine-specific ADP-ribosyltransferase 1, arginine-specific ADP-ribosytransferases 1, arginine-specific mono-ADP-ribosyltransferase, arginine-specific mono-ADP-ribosyltransferase 1, arginine-specific mono-ADP-ribosyltransferase A, ARH1, ART, ART1, ART2, ART3, ART4, ART5, Art7.1, Art7.2, ARTase, ARTC1, ARTD15, ARTD15/PARP16, asparagine-specific ADP-ribosyltransferase, AT1 , AT2 , binary toxin, binary toxin A, binary toxin component Ia, C2 toxin, C2I, cARTC2.1, CD196 ADP-ribosyltransferase, CDT, CdtA, cholera toxin, cholix toxin, CTA, Dombrock blood group carrier molecule , exoenzyme C3, glycosylphosphatidylinositol-anchored arginine-specific ADP-ribosyltransferase7.1, i-toxin, iota toxin, MART-A, mono(ADP-ribosyl)transferase , mono-ADP-ribosyl-arginine hydrolase, mono-ADP-ribosyltransferase, mono-ADP-ribosyltransferase A, NAD(P)+-arginine ADP-ribosyltransferase, NAD+:arginine ADP-ribosyltransferase, NAD+:arginine ecto-mono(ADP-ribosyl)transferase, NAD+:L-arginine ADP-D-ribosyltransferase, NAD-arginine ADP-ribosyltransferase, NAD-arginine mono-ADP-ribosyltransferase B, NAD-dependent ADPribosyltransferase, NAD:arginine ADP-ribosyltransferase, NAD:arginine ADP-ribosyltransferase B, NarE, PARP16/ARTD15, RT6, RT6.1, RT6.2, T-cell surface protein Rt6.1 , T-cell surface protein Rt6.2 , TcdB2-TccC3, VIP2, Vis toxin, XAC3230, XopAI

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.31 NAD+-protein-arginine ADP-ribosyltransferase

Crystallization

Crystallization on EC 2.4.2.31 - NAD+-protein-arginine ADP-ribosyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic subunit CdtA in its native form at pH 4.0, 8.5, and 9.0 and in complex with ADP-ribose donors, NAD+ and NADPH at pH 9.0. The crystal structures of the native protein show pronounced conformational flexibility confined to the active site region of the protein and enhanced disorder at low pH. The suggested catalytically important residues Glu385 and Glu387 seem to play no role or a less important role in ligand binding
high-resolution structures of NAD(+)-iota toxin-actin and iota toxin-ADPR-actin obtained by soaking apo-iota toxin-actin crystal with NAD(+) under different conditions and structures of mutants E378S, E380A, E380S in complex with actin. The structures of NAD(+)-iota toxin-actin and iota toxin-ADPR-actin represent the pre- and postreaction states. A simple strain-alleviation model explains arginine ADP ribosylation occuring via two oxocarbenium ion intermediates
structure of the Ia complex with NADH at 1.8 A. Vapor diffusion method
-
the crystal structure of human ARTD15/PARP16 is shown. ARTD15 features an alpha-helical domain that packs against its transferase domain without making direct contact with the NAD+-binding crevice or the donor loop
apoenzyme and in complex with NAD+ and inhibitors, vapor diffusion method
-
hanging drop vapor diffusion method, using either 15% (w/v) PEG 400, 5.5% (w/v) PEG 20000, and 50 mM KH2PO4, pH 8.0 or 16.5% (w/v) PEG 400, 6.5% (w/v) PEG 20000, and 50 mM KH2PO4, pH 8.0