Three conserved consensus sequences identify the NAD-binding site of ADP-ribosylating enzymes, expressed by eukaryotes, bacteria and T-even bacteriophages.

Abstract:

:It has been previously reported that the three-dimensional structures of the NAD-binding and catalytic site of bacterial toxins with ADP-ribosylating activity are superimposable, and that the key amino acids for the enzymatic activity are conserved. The model includes an NAD-binding and catalytic site formed by an alpha-helix bent over a beta-strand, surrounded by two beta-strands bearing a Glu and a His, or Arg, that are required for catalysis. We show here that the model can be extended to comprise all proteins with ADP-ribosylating activity known to date, including all eukaryotic mono- and poly-ADP-ribosyltransferases, the bacterial ADP-ribosylating enzymes which do not have toxic activity, and the analogous enzymes encoded by T-even bacteriophages. We show that, in addition to the common Glu and Arg/His amino acids previously identified, the conserved motifs can be extended as follows: (i) the Arg/His motif is usually arom-His/Arg (where 'arom' is an aromatic residue); (ii) in the sequences of the CT group the beta-strand forming part of the 'scaffold' of the catalytic cavity has an arom-ph-Ser-Thr-Ser-ph consensus (where 'ph' represents a hydrophobic residue); and (iii) the motif centered in the key glutamic residue is Glu/Gin-X-Glu; while (iv) in the sequences of the DT group the NAD-binding motif is Tyr-X10-Tyr. We believe that the model proposed not only accounts for all ADP-ribosylating proteins known to date, but it is likely to fit other enzymes (currently being analysed) which possess such an activity.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Domenighini M,Rappuoli R

doi

10.1046/j.1365-2958.1996.321396.x

subject

Has Abstract

pub_date

1996-08-01 00:00:00

pages

667-74

issue

4

eissn

0950-382X

issn

1365-2958

journal_volume

21

pub_type

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