1g9q: Difference between revisions

Revision as of 04:57, 1 July 2008

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File:1g9q.png

Template:STRUCTURE 1g9q

COMPLEX STRUCTURE OF THE ADPR-ASE AND ITS SUBSTRATE ADP-RIBOSECOMPLEX STRUCTURE OF THE ADPR-ASE AND ITS SUBSTRATE ADP-RIBOSE

Template:ABSTRACT PUBMED 11323725

About this StructureAbout this Structure

1G9Q is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family., Gabelli SB, Bianchet MA, Bessman MJ, Amzel LM, Nat Struct Biol. 2001 May;8(5):467-72. PMID:11323725

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+===COMPLEX STRUCTURE OF THE ADPR-ASE AND ITS SUBSTRATE ADP-RIBOSE===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11323725}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Gabelli, S B]]
 [[Category: Nudix]]
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