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| | <StructureSection load='5a61' size='340' side='right'caption='[[5a61]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='5a61' size='340' side='right'caption='[[5a61]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5a61]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A61 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A61 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5a61]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A61 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A61 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PO:TRIPHOSPHATE'>3PO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PO:TRIPHOSPHATE'>3PO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a5y|5a5y]], [[5a60|5a60]], [[5a64|5a64]], [[5a65|5a65]], [[5a66|5a66]], [[5a67|5a67]], [[5a68|5a68]]</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=5a61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a61 OCA], [https://pdbe.org/5a61 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a61 RCSB], [https://www.ebi.ac.uk/pdbsum/5a61 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a61 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triphosphatase Triphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.25 3.6.1.25] </span></td></tr>
| + | |
| - | <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=5a61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a61 OCA], [http://pdbe.org/5a61 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a61 RCSB], [http://www.ebi.ac.uk/pdbsum/5a61 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a61 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/3PASE_ECOLI 3PASE_ECOLI] Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi), which could be cytotoxic because of its high affinity for calcium ion, thereby interfering with calcium signaling. It also hydrolyzes slowly thiamine triphosphate (ThTP). YgiF is a specific PPPase, but it contributes only marginally to the total PPPase activity in E.coli, where the main enzyme responsible for hydrolysis of PPPi is inorganic pyrophosphatase (PPase).<ref>PMID:22984449</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Triphosphatase]]
| + | [[Category: Hothorn M]] |
| - | [[Category: Hothorn, M]] | + | [[Category: Martinez J]] |
| - | [[Category: Martinez, J]] | + | [[Category: Truffault V]] |
| - | [[Category: Truffault, V]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Triphosphate tunnel metalloenzyme]]
| + | |
| - | [[Category: Tripolyphosphate]]
| + | |
| Structural highlights
Function
3PASE_ECOLI Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi), which could be cytotoxic because of its high affinity for calcium ion, thereby interfering with calcium signaling. It also hydrolyzes slowly thiamine triphosphate (ThTP). YgiF is a specific PPPase, but it contributes only marginally to the total PPPase activity in E.coli, where the main enzyme responsible for hydrolysis of PPPi is inorganic pyrophosphatase (PPase).[1]
Publication Abstract from PubMed
Triphosphate tunnel metalloenzymes (TTMs) are present in all kingdoms of life and catalyze diverse enzymatic reactions such as mRNA capping, the cyclization of adenosine triphosphate, the hydrolysis of thiamine triphosphate and the synthesis and breakdown of inorganic polyphosphates. TTMs have an unusual tunnel domain fold that harbors substrate- and metal co-factor binding sites. It is presently poorly understood how TTMs specifically sense different triphosphate-containing substrates and how catalysis occurs in the tunnel center. Here we describe substrate-bound structures of inorganic polyphosphatases from Arabidopsis and E. coli, which reveal an unorthodox yet conserved mode of triphosphate and metal co-factor binding. We identify two metal binding sites in these enzymes, with one co-factor involved in substrate coordination and the other in catalysis. Structural comparisons with a substrate- and product-bound mammalian thiamine triphosphatase, and with previously reported structures of mRNA capping enzymes, adenylate cyclases and polyphosphate polymerases, suggest that directionality of substrate binding defines TTM catalytic activity. Our work provides insight into the evolution and functional diversification of an ancient enzyme family.
Structural Determinants for Substrate Binding and Catalysis in Triphosphate Tunnel Metalloenzymes.,Martinez J, Truffault V, Hothorn M J Biol Chem. 2015 Jul 28. pii: jbc.M115.674473. PMID:26221030[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kohn G, Delvaux D, Lakaye B, Servais AC, Scholer G, Fillet M, Elias B, Derochette JM, Crommen J, Wins P, Bettendorff L. High inorganic triphosphatase activities in bacteria and mammalian cells: identification of the enzymes involved. PLoS One. 2012;7(9):e43879. PMID:22984449 doi:10.1371/journal.pone.0043879
- ↑ Martinez J, Truffault V, Hothorn M. Structural Determinants for Substrate Binding and Catalysis in Triphosphate Tunnel Metalloenzymes. J Biol Chem. 2015 Jul 28. pii: jbc.M115.674473. PMID:26221030 doi:http://dx.doi.org/10.1074/jbc.M115.674473
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