1j9k: Difference between revisions
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<StructureSection load='1j9k' size='340' side='right'caption='[[1j9k]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1j9k' size='340' side='right'caption='[[1j9k]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1j9k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1j9k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J9K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J9K FirstGlance]. <br> | ||
</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>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=WO4:TUNGSTATE(VI)ION'>WO4</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=WO4:TUNGSTATE(VI)ION'>WO4</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=1j9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j9k OCA], [https://pdbe.org/1j9k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j9k RCSB], [https://www.ebi.ac.uk/pdbsum/1j9k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j9k ProSAT]</span></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=1j9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j9k OCA], [https://pdbe.org/1j9k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j9k RCSB], [https://www.ebi.ac.uk/pdbsum/1j9k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j9k ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SURE_THEMA SURE_THEMA] Nucleotidase that preferentially dephosphorylates 5'-GMP and 5'-AMP.[HAMAP-Rule:MF_00060] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermotoga maritima]] | ||
[[Category: | [[Category: Kwak JE]] | ||
[[Category: | [[Category: Lee JY]] | ||
[[Category: | [[Category: Moon J]] | ||
[[Category: | [[Category: Suh SW]] | ||
Latest revision as of 10:14, 25 October 2023
CRYSTAL STRUCTURE OF SURE PROTEIN FROM T.MARITIMA IN COMPLEX WITH TUNGSTATECRYSTAL STRUCTURE OF SURE PROTEIN FROM T.MARITIMA IN COMPLEX WITH TUNGSTATE
Structural highlights
FunctionSURE_THEMA Nucleotidase that preferentially dephosphorylates 5'-GMP and 5'-AMP.[HAMAP-Rule:MF_00060] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHomologs of the Escherichia coli surE gene are present in many eubacteria and archaea. Despite the evolutionary conservation, little information is available on the structure and function of their gene products. We have determined the crystal structure of the SurE protein from Thermotoga maritima. The structure reveals the dimeric arrangement of the subunits and an active site around a bound metal ion. We also demonstrate that the SurE protein exhibits a divalent metal ion-dependent phosphatase activity that is inhibited by vanadate or tungstate. In the vanadate- and tungstate-complexed structures, the inhibitors bind adjacent to the divalent metal ion. Our structural and functional analyses identify the SurE proteins as a novel family of metal ion-dependent phosphatases. Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family.,Lee JY, Kwak JE, Moon J, Eom SH, Liong EC, Pedelacq JD, Berendzen J, Suh SW Nat Struct Biol. 2001 Sep;8(9):789-94. PMID:11524683[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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