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| | <StructureSection load='5gkx' size='340' side='right'caption='[[5gkx]], [[Resolution|resolution]] 2.01Å' scene=''> | | <StructureSection load='5gkx' size='340' side='right'caption='[[5gkx]], [[Resolution|resolution]] 2.01Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gkx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Theon Theon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GKX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GKX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gkx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_onnurineus_NA1 Thermococcus onnurineus NA1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GKX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GKX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fc5|4fc5]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TON_0340 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=523850 THEON])</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=5gkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gkx OCA], [https://pdbe.org/5gkx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gkx RCSB], [https://www.ebi.ac.uk/pdbsum/5gkx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gkx ProSAT]</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=5gkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gkx OCA], [http://pdbe.org/5gkx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gkx RCSB], [http://www.ebi.ac.uk/pdbsum/5gkx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gkx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B6YTD8_THEON B6YTD8_THEON] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Theon]] | + | [[Category: Thermococcus onnurineus NA1]] |
| - | [[Category: Lee, S G]] | + | [[Category: Lee SG]] |
| - | [[Category: Oh, B H]] | + | [[Category: Oh BH]] |
| - | [[Category: Sohn, Y S]] | + | [[Category: Sohn YS]] |
| - | [[Category: Mn2+-dependent phosphatase]]
| + | |
| - | [[Category: Thermococcus onnurineus]]
| + | |
| - | [[Category: Ton_0340]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
B6YTD8_THEON
Publication Abstract from PubMed
A hypothetical protein TON_0340 of a Thermococcus species is a protein conserved in a variety of organisms including human. Herein, we present four different crystal structures of TON_0340, leading to the identification of an active-site cavity harboring a metal-binding site composed of six invariant aspartate and glutamate residues that coordinate one to three metal ions. Biochemical and mutational analyses involving many phosphorous compounds show that TON_0340 is a Mn2+-dependent phosphatase. Mg2+ binds to TON_0340 less tightly and activates the phosphatase activity less efficiently than Mn2+. Whereas Ca2+ and Zn2+ are able to bind to the protein, they are unable to activate its enzymatic activity. Since the active-site cavity is small and largely composed of nearly invariant stretches of 11 or 13 amino acids, the physiological substrates of TON_0340 and its homologues are likely to be a small and the same molecule. The Mn2+-bound TON_0340 structure provides a canonical model for the ubiquitously present TON_0340 homologues and lays a strong foundation for the elucidation of their substrate and biological function.
Identification of a Highly Conserved Hypothetical Protein TON_0340 as a Probable Manganese-Dependent Phosphatase.,Sohn YS, Lee SG, Lee KH, Ku B, Shin HC, Cha SS, Kim YG, Lee HS, Kang SG, Oh BH PLoS One. 2016 Dec 1;11(12):e0167549. doi: 10.1371/journal.pone.0167549., eCollection 2016. PMID:27907125[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sohn YS, Lee SG, Lee KH, Ku B, Shin HC, Cha SS, Kim YG, Lee HS, Kang SG, Oh BH. Identification of a Highly Conserved Hypothetical Protein TON_0340 as a Probable Manganese-Dependent Phosphatase. PLoS One. 2016 Dec 1;11(12):e0167549. doi: 10.1371/journal.pone.0167549., eCollection 2016. PMID:27907125 doi:http://dx.doi.org/10.1371/journal.pone.0167549
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