2h2u

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{{Seed}}
 
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[[Image:2h2u.png|left|200px]]
 
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==Crystal structure of the E130Y mutant of human soluble calcium-activated nucleotidase (SCAN) with calcium ion==
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The line below this paragraph, containing "STRUCTURE_2h2u", creates the "Structure Box" on the page.
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<StructureSection load='2h2u' size='340' side='right'caption='[[2h2u]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2h2u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H2U FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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{{STRUCTURE_2h2u| PDB=2h2u | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2u OCA], [https://pdbe.org/2h2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h2u RCSB], [https://www.ebi.ac.uk/pdbsum/2h2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h2u ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/CANT1_HUMAN CANT1_HUMAN] Desbuquois syndrome. The disease is caused by mutations affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/CANT1_HUMAN CANT1_HUMAN] Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis.<ref>PMID:12234496</ref> <ref>PMID:15248776</ref> <ref>PMID:22539336</ref>
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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/h2/2h2u_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/main_output.php?pdb_ID=2h2u 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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Mammals express a protein homologous to soluble nucleotidases used by blood-sucking insects to inhibit host blood clotting. These vertebrate nucleotidases may play a role in protein glycosylation. The activity of this enzyme family is strictly dependent on calcium, which induces a conformational change in the secreted, soluble human nucleotidase. The crystal structure of this human enzyme was recently solved; however, the mechanism of calcium activation and the basis for the calcium-induced changes remain unclear. In this study, using analytical ultracentrifugation and chemical cross-linking, we show that calcium or strontium induce noncovalent dimerization of the soluble human enzyme. The location and nature of the dimer interface was elucidated using a combination of site-directed mutagenesis and chemical cross-linking, coupled with crystallographic analyses. Replacement of Ile(170), Ser(172), and Ser(226) with cysteine residues resulted in calcium-dependent, sulfhydryl-specific intermolecular cross-linking, which was not observed after cysteine introduction at other surface locations. Analysis of a super-active mutant, E130Y, revealed that this mutant dimerized more readily than the wild-type enzyme. The crystal structure of the E130Y mutant revealed that the mutated residue is found in the dimer interface. In addition, expression of the full-length nucleotidase revealed that this membrane-bound form can also dimerize and that these dimers are stabilized by spontaneous oxidative cross-linking of Cys(30), located between the single transmembrane helix and the start of the soluble sequence. Thus, calcium-mediated dimerization may also represent a mechanism for regulation of the activity of this nucleotidase in the physiological setting of the endoplasmic reticulum or Golgi.
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===Crystal structure of the E130Y mutant of human soluble calcium-activated nucleotidase (SCAN) with calcium ion===
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Calcium-dependent dimerization of human soluble calcium activated nucleotidase: characterization of the dimer interface.,Yang M, Horii K, Herr AB, Kirley TL J Biol Chem. 2006 Sep 22;281(38):28307-17. Epub 2006 Jul 11. PMID:16835225<ref>PMID:16835225</ref>
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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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The line below this paragraph, {{ABSTRACT_PUBMED_16835225}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2h2u" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16835225 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16835225}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2H2U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H2U OCA].
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==Reference==
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Calcium-dependent dimerization of human soluble calcium activated nucleotidase: characterization of the dimer interface., Yang M, Horii K, Herr AB, Kirley TL, J Biol Chem. 2006 Sep 22;281(38):28307-17. Epub 2006 Jul 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16835225 16835225]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Nucleoside-diphosphatase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Herr AB]]
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[[Category: Herr, A B.]]
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[[Category: Horii K]]
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[[Category: Horii, K.]]
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[[Category: Kirley TL]]
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[[Category: Kirley, T L.]]
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[[Category: Yang M]]
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[[Category: Yang, M.]]
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[[Category: Calcium-binding protein]]
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[[Category: Five-blade beta propeller]]
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[[Category: Nucleotidase]]
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[[Category: Nucleotide-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:26:34 2008''
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Current revision

Crystal structure of the E130Y mutant of human soluble calcium-activated nucleotidase (SCAN) with calcium ion

PDB ID 2h2u

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