1g9q: Difference between revisions

Revision as of 13:47, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

1G9Q is a Single protein structure of sequence from Escherichia coli with as ligand. Active as ADP-ribose diphosphatase, with EC number 3.6.1.13 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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OCA

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-[[Image:1g9q.jpg|left|200px]]<br /><applet load="1g9q" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1g9q.jpg|left|200px]]<br /><applet load="1g9q" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1g9q, resolution 2.30&Aring;" />
 '''COMPLEX STRUCTURE OF THE ADPR-ASE AND ITS SUBSTRATE ADP-RIBOSE'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-G9Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with APR as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/ADP-ribose_diphosphatase ADP-ribose diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.13 3.6.1.13] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G9Q OCA].
+G9Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=APR:'>APR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/ADP-ribose_diphosphatase ADP-ribose diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.13 3.6.1.13] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G9Q OCA].
 ==Reference==
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 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Amzel, L.M.]]
+[[Category: Amzel, L M.]]
-[[Category: Bessman, M.J.]]
+[[Category: Bessman, M J.]]
-[[Category: Bianchet, M.A.]]
+[[Category: Bianchet, M A.]]
-[[Category: Gabelli, S.B]]
+[[Category: Gabelli, S B]]
 [[Category: APR]]
 [[Category: nudix]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:51:39 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:46 2008''