7btn: Difference between revisions

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-'''Unreleased structure'''
-The entry 7btn is ON HOLD  until Apr 02 2022
+==Crystal structure of human inorganic pyrophosphatase with metal ions==
+<StructureSection load='7btn' size='340' side='right'caption='[[7btn]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7btn]] is a 1 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=7BTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BTN FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.382&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7btn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7btn OCA], [https://pdbe.org/7btn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7btn RCSB], [https://www.ebi.ac.uk/pdbsum/7btn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7btn ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/IPYR_HUMAN IPYR_HUMAN]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Inorganic pyrophosphatase (PPase) plays an essential role in energy conservation and provides energy for many biosynthetic pathways. Here, we present two three-dimensional structures of PPase from Homo sapiens (Hu-PPase) at 2.38 A and 3.40 A in different crystallization conditions. One of the Hu-PPase structures complex of two magnesium metal ions was determined to be a monomer (Hu-PPase-mono) here, while the other one to be a dimer-dimer (Hu-PPase-dd). In each asymmetric unit of Hu-PPase-mono, there are four alpha-helices and ten beta-strands and folds as a barrel structure, and the active site contains two magnesium ions. Like PPases from many species, we found that Hu-PPase was able to undergo self-assembly. To our surprise, disruption of the self-assembly of Hu-PPase did not influence its enzymatic activity or the ability to promote cell growth. Our work uncovered that different structure forms of Hu-PPase and found that the pyrophosphatase activity of Hu-PPase is independent of its self-assembly.
-Authors: Hu, F., Huang, Z., Li, L.
+Structural and biochemical characterization of inorganic pyrophosphatase from Homo sapiens.,Hu F, Huang Z, Zheng S, Wu Q, Chen Y, Lin H, Huang W, Li L Biochem Biophys Res Commun. 2020 Oct 6. pii: S0006-291X(20)31891-X. doi:, 10.1016/j.bbrc.2020.09.139. PMID:33036755<ref>PMID:33036755</ref>
-Description: Crystal structure of human inorganic pyrophosphatase with metal ions
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Huang, Z]]
+<div class="pdbe-citations 7btn" style="background-color:#fffaf0;"></div>
-[[Category: Hu, F]]
-[[Category: Li, L]]
+==See Also==
+*[[Inorganic pyrophosphatase 3D structures|Inorganic pyrophosphatase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Hu F]]
+[[Category: Huang Z]]
+[[Category: Li L]]