1G0S

THE CRYSTAL STRUCTURE OF THE E.COLI ADP-RIBOSE PYROPHOSPHATASE

Summary for 1G0S

• Entry DOI: 10.2210/pdb1g0s/pdb
• Descriptor: HYPOTHETICAL 23.7 KDA PROTEIN IN ICC-TOLC INTERGENIC REGION (2 entities in total)
• Functional Keywords: nudix fold, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 47391.56

Authors

Gabelli, S.B.,Bianchet, M.A.,Bessman, M.J.,Amzel, L.M. (deposition date: 2000-10-08, release date: 2001-05-02, Last modification date: 2024-02-07)

Primary citation

Gabelli, S.B.,Bianchet, M.A.,Bessman, M.J.,Amzel, L.M.
The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family.
Nat.Struct.Biol., 8:467-472, 2001

PubMed 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.

PubMed: 11323725
DOI: 10.1038/87647

Experimental method

X-RAY DIFFRACTION (1.9 Å)