PMID:11323725
| Citation |
Gabelli, SB, Bianchet, MA, Bessman, MJ and Amzel, LM (2001) The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family. Nat. Struct. Biol. 8:467-72 |
|---|---|
| Abstract |
Regulation of cellular levels of ADP-ribose is important in preventing nonenzymatic ADP-ribosylation of proteins. The Escherichia coli ADP-ribose pyrophosphatase, a Nudix enzyme, catalyzes the hydrolysis of ADP-ribose to ribose-5-P and AMP, compounds that can be recycled as part of nucleotide metabolism. The structures of the apo enzyme, the active enzyme and the complex with ADP-ribose were determined to 1.9 A, 2.7 A and 2.3 A, respectively. The structures reveal a symmetric homodimer with two equivalent catalytic sites, each formed by residues of both monomers, requiring dimerization through domain swapping for substrate recognition and catalytic activity. The structures also suggest a role for the residues conserved in each Nudix subfamily. The Nudix motif residues, folded as a loop-helix-loop tailored for pyrophosphate hydrolysis, compose the catalytic center; residues conferring substrate specificity occur in regions of the sequence removed from the Nudix motif. This segregation of catalytic and recognition roles provides versatility to the Nudix family. |
| Links |
PubMed Online version:10.1038/87647 |
| Keywords |
Adenosine Diphosphate Ribose/metabolism; Amino Acid Motifs; Amino Acid Sequence; Apoenzymes/chemistry; Apoenzymes/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding Sites; Cations, Divalent/metabolism; Conserved Sequence; Crystallography, X-Ray; Dimerization; Enzyme Activation; Escherichia coli/enzymology; Escherichia coli Proteins; Hydrolysis; Magnesium/metabolism; Models, Molecular; Molecular Sequence Data; Phosphoric Monoester Hydrolases/chemistry; Phosphoric Monoester Hydrolases/metabolism; Protein Structure, Tertiary; Pyrophosphatases/chemistry; Pyrophosphatases/metabolism; Sequence Alignment; Structure-Activity Relationship; Substrate Specificity |
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