1lk5: Difference between revisions

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 <StructureSection load='1lk5' size='340' side='right'caption='[[1lk5]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1lk5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/'pyrococcus_shinkaii' 'pyrococcus shinkaii']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LK5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LK5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1lk5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LK5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LK5 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.75&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lk7|1lk7]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribose-5-phosphate_isomerase Ribose-5-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.6 5.3.1.6] </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=1lk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lk5 OCA], [https://pdbe.org/1lk5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lk5 RCSB], [https://www.ebi.ac.uk/pdbsum/1lk5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lk5 ProSAT]</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=1lk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lk5 OCA], [http://pdbe.org/1lk5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lk5 RCSB], [http://www.ebi.ac.uk/pdbsum/1lk5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lk5 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/RPIA_PYRHO RPIA_PYRHO]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 20: @@
 </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=1lk5 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-A gene homologous to D-ribose-5-phosphate isomerase (EC 5.3.1.6) was found in the genome of Pyrococcus horikoshii. D-ribose-5-phosphate isomerase (PRI) is of particular metabolic importance since it catalyzes the interconversion between the ribose and ribulose forms involved in the pentose phosphate cycle and in the process of photosynthesis. The gene consisting of 687 bp was overexpressed in Escherichia coli, and the resulting enzyme showed activity at high temperatures with an optimum over 90 degrees C. The crystal structures of the enzyme, free and in complex with D-4-phosphoerythronic acid inhibitor, were determined. PRI is a tetramer in the crystal and in solution, and each monomer has a new fold consisting of two alpha/beta domains. The 3D structures and the characterization of different mutants indicate a direct or indirect catalytic role for the residues E107, D85, and K98.
-A hyperthermostable D-ribose-5-phosphate isomerase from Pyrococcus horikoshii characterization and three-dimensional structure.,Ishikawa K, Matsui I, Payan F, Cambillau C, Ishida H, Kawarabayasi Y, Kikuchi H, Roussel A Structure. 2002 Jun;10(6):877-86. PMID:12057201<ref>PMID:12057201</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1lk5" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Ribose-5-phosphate isomerase|Ribose-5-phosphate isomerase]]
+*[[Ribose-5-phosphate isomerase 3D structures|Ribose-5-phosphate isomerase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Pyrococcus shinkaii]]
 [[Category: Large Structures]]
-[[Category: Ribose-5-phosphate isomerase]]
+[[Category: Pyrococcus horikoshii]]
-[[Category: Cambillau, C]]
+[[Category: Cambillau C]]
-[[Category: Ishida, H]]
+[[Category: Ishida H]]
-[[Category: Ishikawa, K]]
+[[Category: Ishikawa K]]
-[[Category: Kawarabayasi, Y]]
+[[Category: Kawarabayasi Y]]
-[[Category: Kikuchi, H]]
+[[Category: Kikuchi H]]
-[[Category: Matsui, I]]
+[[Category: Matsui I]]
-[[Category: Payan, F]]
+[[Category: Payan F]]
-[[Category: Roussel, A]]
+[[Category: Roussel A]]
-[[Category: Alpha/beta structure]]
-[[Category: Isomerase]]

1lk5: Difference between revisions

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