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[[Image:1g0s.jpg|left|200px]]


{{Structure
==THE CRYSTAL STRUCTURE OF THE E.COLI ADP-RIBOSE PYROPHOSPHATASE==
|PDB= 1g0s |SIZE=350|CAPTION= <scene name='initialview01'>1g0s</scene>, resolution 1.9&Aring;
<StructureSection load='1g0s' size='340' side='right'caption='[[1g0s]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1g0s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G0S FirstGlance]. <br>
|ACTIVITY= [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]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0s OCA], [https://pdbe.org/1g0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g0s RCSB], [https://www.ebi.ac.uk/pdbsum/1g0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g0s ProSAT]</span></td></tr>
}}
</table>
 
== Function ==
'''THE CRYSTAL STRUCTURE OF THE E.COLI ADP-RIBOSE PYROPHOSPHATASE'''
[https://www.uniprot.org/uniprot/ADPP_ECOLI ADPP_ECOLI] Acts on ADP-mannose and ADP-glucose as well as ADP-ribose. Prevents glycogen biosynthesis. The reaction catalyzed by this enzyme is a limiting step of the gluconeogenic process.<ref>PMID:11416161</ref>
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
==Overview==
Check<jmol>
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.
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g0/1g0s_consurf.spt"</scriptWhenChecked>
==About this Structure==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
1G0S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0S OCA].  
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==Reference==
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1g0s ConSurf].
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:[http://www.ncbi.nlm.nih.gov/pubmed/11323725 11323725]
<div style="clear:both"></div>
[[Category: ADP-ribose diphosphatase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Amzel, L M.]]
[[Category: Amzel LM]]
[[Category: Bessman, M J.]]
[[Category: Bessman MJ]]
[[Category: Bianchet, M A.]]
[[Category: Bianchet MA]]
[[Category: Gabelli, S B.]]
[[Category: Gabelli SB]]
[[Category: nudix fold]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:16:35 2008''

Latest revision as of 07:21, 7 February 2024

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

1g0s, resolution 1.90Å

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