5gl2: Difference between revisions

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'''Unreleased structure'''


The entry 5gl2 is ON HOLD
==Crystal structure of TON_0340 in complex with Ca==
<StructureSection load='5gl2' size='340' side='right'caption='[[5gl2]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5gl2]] is a 6 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=5GL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GL2 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]] 2.03&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5gl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gl2 OCA], [https://pdbe.org/5gl2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gl2 RCSB], [https://www.ebi.ac.uk/pdbsum/5gl2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gl2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B6YTD8_THEON B6YTD8_THEON]
<div style="background-color:#fffaf0;">
== 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.


Authors: Lee, S.G., Sohn, Y.S., Oh, B.H.
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<ref>PMID:27907125</ref>


Description: Crystal structure of TON_0340
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Oh, B.H]]
<div class="pdbe-citations 5gl2" style="background-color:#fffaf0;"></div>
[[Category: Sohn, Y.S]]
== References ==
[[Category: Lee, S.G]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermococcus onnurineus NA1]]
[[Category: Lee SG]]
[[Category: Oh BH]]
[[Category: Sohn YS]]
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