1j3q
From Proteopedia
(Difference between revisions)
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<StructureSection load='1j3q' size='340' side='right'caption='[[1j3q]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='1j3q' size='340' side='right'caption='[[1j3q]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1j3q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1j3q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_litoralis Thermococcus litoralis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J3Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J3Q FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1j3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j3q OCA], [https://pdbe.org/1j3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j3q RCSB], [https://www.ebi.ac.uk/pdbsum/1j3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j3q 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=1j3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j3q OCA], [https://pdbe.org/1j3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j3q RCSB], [https://www.ebi.ac.uk/pdbsum/1j3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j3q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/G6PI_THELI G6PI_THELI] | ||
== 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=1j3q 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=1j3q ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The gene encoding phosphoglucose isomerase was cloned from Thermococcus litoralis, and functionally expressed in Escherichia coli. The purified enzyme, a homodimer of 21.5 kDa subunits, was biochemically characterized. The inhibition constants for four competitive inhibitors were determined. The enzyme contained 1.25 mol Fe and 0.24 mol Zn per dimer. The activity was enhanced by the addition of Fe(2+), but inhibited by Zn(2+) and EDTA. Enzymes with mutations in conserved histidine and glutamate residues in their cupin motifs contained no metals, and showed large decreases in k(cat). The circular dichroism spectra of the mutant enzymes and the wild type enzyme were essentially the same but with slight differences. | ||
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- | Characterization of the cupin-type phosphoglucose isomerase from the hyperthermophilic archaeon Thermococcus litoralis.,Jeong JJ, Fushinobu S, Ito S, Jeon BS, Shoun H, Wakagi T FEBS Lett. 2003 Jan 30;535(1-3):200-4. PMID:12560104<ref>PMID:12560104</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1j3q" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Phosphoglucose isomerase 3D structures|Phosphoglucose isomerase 3D structures]] | *[[Phosphoglucose isomerase 3D structures|Phosphoglucose isomerase 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Caldococcus litoralis z-1301]] | ||
- | [[Category: Glucose-6-phosphate isomerase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Fushinobu | + | [[Category: Thermococcus litoralis]] |
- | [[Category: Hidaka | + | [[Category: Fushinobu S]] |
- | [[Category: Ito | + | [[Category: Hidaka M]] |
- | [[Category: Jeong | + | [[Category: Ito S]] |
- | [[Category: Shoun | + | [[Category: Jeong J-J]] |
- | [[Category: Wakagi | + | [[Category: Shoun H]] |
- | + | [[Category: Wakagi T]] | |
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Current revision
Crystal structure of Thermococcus litoralis phosphogrucose isomerase soaked with FeSO4
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