1j9j: Difference between revisions

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<StructureSection load='1j9j' size='340' side='right'caption='[[1j9j]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1j9j' size='340' side='right'caption='[[1j9j]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1j9j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J9J FirstGlance]. <br>
<table><tr><td colspan='2'>[[1j9j]] 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=1J9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J9J FirstGlance]. <br>
</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.9&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1j9k|1j9k]], [[1j9l|1j9l]]</div></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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1j9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j9j OCA], [https://pdbe.org/1j9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j9j RCSB], [https://www.ebi.ac.uk/pdbsum/1j9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j9j 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=1j9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j9j OCA], [https://pdbe.org/1j9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j9j RCSB], [https://www.ebi.ac.uk/pdbsum/1j9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j9j 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]  
[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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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1j9j ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1j9j ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Homologs 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<ref>PMID:11524683</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1j9j" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43589]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kwak, J E]]
[[Category: Lee, J Y]]
[[Category: Moon, J]]
[[Category: Suh, S W]]
[[Category: Sure protein]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Unknown function]]
[[Category: Kwak JE]]
[[Category: Lee JY]]
[[Category: Moon J]]
[[Category: Suh SW]]

Latest revision as of 16:24, 13 March 2024

CRYSTAL STRUCTURE ANALYSIS OF SURE PROTEIN FROM T.MARITIMACRYSTAL STRUCTURE ANALYSIS OF SURE PROTEIN FROM T.MARITIMA

Structural highlights

1j9j is a 2 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SURE_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.

1j9j, resolution 1.90Å

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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