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==Crystal structure of human inorganic pyrophosphatase with metal ions== | ==Crystal structure of human inorganic pyrophosphatase with metal ions== | ||
<StructureSection load='7btn' size='340' side='right'caption='[[7btn]]' scene=''> | <StructureSection load='7btn' size='340' side='right'caption='[[7btn]], [[Resolution|resolution]] 2.38Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>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 [http://proteopedia.org/fgij/fg.htm?mol=7BTN FirstGlance]. <br> | <table><tr><td colspan='2'>[[7btn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://proteopedia.org/fgij/fg.htm?mol=7BTN FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7btn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7btn OCA], [http://pdbe.org/7btn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7btn RCSB], [http://www.ebi.ac.uk/pdbsum/7btn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7btn ProSAT]</span></td></tr> | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPA1, IOPPP, PP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Inorganic_diphosphatase Inorganic diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.1 3.6.1.1] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7btn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7btn OCA], [http://pdbe.org/7btn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7btn RCSB], [http://www.ebi.ac.uk/pdbsum/7btn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7btn ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7btn" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Inorganic diphosphatase]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hu F]] | [[Category: Hu, F]] | ||
[[Category: Huang Z]] | [[Category: Huang, Z]] | ||
[[Category: Li L]] | [[Category: Li, L]] | ||
[[Category: Complex]] | |||
[[Category: Hydrolase]] | |||
[[Category: Monomer]] | |||
Revision as of 10:03, 30 December 2020
Crystal structure of human inorganic pyrophosphatase with metal ionsCrystal structure of human inorganic pyrophosphatase with metal ions
Structural highlights
Publication Abstract from PubMedInorganic 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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