1j3r: Difference between revisions
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<StructureSection load='1j3r' size='340' side='right' caption='[[1j3r]], [[Resolution|resolution]] 2.18Å' scene=''> | <StructureSection load='1j3r' size='340' side='right' caption='[[1j3r]], [[Resolution|resolution]] 2.18Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1j3r]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1j3r]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/'caldococcus_litoralis'_z-1301 'caldococcus litoralis' z-1301]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J3R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J3R FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6PG:6-PHOSPHOGLUCONIC+ACID'>6PG</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6PG:6-PHOSPHOGLUCONIC+ACID'>6PG</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1j3p|1j3p]], [[1j3q|1j3q]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1j3p|1j3p]], [[1j3q|1j3q]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase Glucose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 5.3.1.9] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j3r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1j3r RCSB], [http://www.ebi.ac.uk/pdbsum/1j3r PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j3r OCA], [http://pdbe.org/1j3r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j3r RCSB], [http://www.ebi.ac.uk/pdbsum/1j3r PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1j3r" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Caldococcus litoralis z-1301]] | |||
[[Category: Glucose-6-phosphate isomerase]] | [[Category: Glucose-6-phosphate isomerase]] | ||
[[Category: Fushinobu, S]] | [[Category: Fushinobu, S]] | ||
[[Category: Hidaka, M]] | [[Category: Hidaka, M]] | ||
Revision as of 06:52, 11 September 2015
Crystal structure of Thermococcus litoralis phosphogrucose isomerase complexed with gluconate-6-phosphateCrystal structure of Thermococcus litoralis phosphogrucose isomerase complexed with gluconate-6-phosphate
Structural highlights
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 PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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