2g0a

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==X-ray structure of mouse pyrimidine 5'-nucleotidase type 1 with lead(II) bound in active site==
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[[Image:2g0a.png|left|200px]]
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<StructureSection load='2g0a' size='340' side='right' caption='[[2g0a]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2g0a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G0A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2G0A FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bdu|2bdu]], [[2g06|2g06]], [[2g07|2g07]], [[2g08|2g08]], [[2g09|2g09]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NT5C3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysophospholipase Lysophospholipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.5 3.1.1.5] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g0a OCA], [http://pdbe.org/2g0a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2g0a RCSB], [http://www.ebi.ac.uk/pdbsum/2g0a PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/5NT3_MOUSE 5NT3_MOUSE]] Can act both as nucleotidase and as phosphotransferase (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g0/2g0a_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Eukaryotic pyrimidine 5'-nucleotidase type 1 (P5N-1) catalyzes dephosphorylation of pyrimidine 5'-mononucleotides. Deficiency of P5N-1 activity in red blood cells results in nonspherocytic hemolytic anemia. The enzyme deficiency is either familial or can be acquired through lead poisoning. We present the crystal structure of mouse P5N-1 refined to 2.35 A resolution. The mouse P5N-1 has a 92% sequence identity to its human counterpart. The structure revealed that P5N-1 adopts a fold similar to enzymes of the haloacid dehydrogenase superfamily. The active site of this enzyme is structurally highly similar to those of phosphoserine phosphatases. We propose a catalytic mechanism for P5N-1 that is also similar to that of phosphoserine phosphatases and provide experimental evidence for the mechanism in the form of structures of several reaction cycle states, including: 1) P5N-1 with bound Mg(II) at 2.25 A, 2) phosphoenzyme intermediate analog at 2.30 A, 3) product-transition complex analog at 2.35 A, and 4) product complex at 2.1A resolution with phosphate bound in the active site. Furthermore the structure of Pb(II)-inhibited P5N-1 (at 2.35 A) revealed that Pb(II) binds within the active site in a way that compromises function of the cationic cavity, which is required for the recognition and binding of the phosphate group of nucleotides.
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<!--
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Structure of pyrimidine 5'-nucleotidase type 1. Insight into mechanism of action and inhibition during lead poisoning.,Bitto E, Bingman CA, Wesenberg GE, McCoy JG, Phillips GN Jr J Biol Chem. 2006 Jul 21;281(29):20521-9. Epub 2006 May 3. PMID:16672222<ref>PMID:16672222</ref>
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The line below this paragraph, containing "STRUCTURE_2g0a", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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-->
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{{STRUCTURE_2g0a| PDB=2g0a | SCENE= }}
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===X-ray structure of mouse pyrimidine 5'-nucleotidase type 1 with lead(II) bound in active site===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2g0a" style="background-color:#fffaf0;"></div>
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<!--
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== References ==
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The line below this paragraph, {{ABSTRACT_PUBMED_16672222}}, adds the Publication Abstract to the page
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<references/>
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(as it appears on PubMed at http://www.pubmed.gov), where 16672222 is the PubMed ID number.
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__TOC__
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</StructureSection>
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{{ABSTRACT_PUBMED_16672222}}
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[[Category: Lk3 transgenic mice]]
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==About this Structure==
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2G0A is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G0A OCA].
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==Reference==
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<ref group="xtra">PMID:16672222</ref><references group="xtra"/>
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[[Category: Lysophospholipase]]
[[Category: Lysophospholipase]]
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[[Category: Mus musculus]]
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[[Category: Bingman, C A]]
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[[Category: Bingman, C A.]]
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[[Category: Bitto, E]]
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[[Category: Bitto, E.]]
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[[Category: Structural genomic]]
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[[Category: CESG, Center for Eukaryotic Structural Genomics.]]
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[[Category: Phillips, G N]]
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[[Category: Jr., G N.Phillips.]]
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[[Category: Wesenberg, G E]]
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[[Category: Wesenberg, G E.]]
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[[Category: Aah38029]]
[[Category: Aah38029]]
[[Category: Bc038029]]
[[Category: Bc038029]]
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[[Category: Center for eukaryotic structural genomic]]
 
[[Category: Cesg]]
[[Category: Cesg]]
[[Category: Cytosolic 5'-nucleotidase iii]]
[[Category: Cytosolic 5'-nucleotidase iii]]
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[[Category: Hydrolase]]
[[Category: Lead poisoning]]
[[Category: Lead poisoning]]
[[Category: Mm 158936]]
[[Category: Mm 158936]]
[[Category: Nt5c3 protein]]
[[Category: Nt5c3 protein]]
[[Category: P5n-1]]
[[Category: P5n-1]]
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[[Category: Protein structure initiative]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Psi]]
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[[Category: Pyrimidine 5'-nucleotidase 1]]
[[Category: Pyrimidine 5'-nucleotidase 1]]
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[[Category: Structural genomics functional follow-up study]]
 
[[Category: Umph-1]]
[[Category: Umph-1]]
[[Category: Uniprot q9d020]]
[[Category: Uniprot q9d020]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 04:18:06 2009''
 

Current revision

X-ray structure of mouse pyrimidine 5'-nucleotidase type 1 with lead(II) bound in active site

2g0a, resolution 2.35Å

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