1lk5

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[[Image:1lk5.jpg|left|200px]]
 
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{{Structure
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==Structure of the D-Ribose-5-Phosphate Isomerase from Pyrococcus horikoshii==
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|PDB= 1lk5 |SIZE=350|CAPTION= <scene name='initialview01'>1lk5</scene>, resolution 1.75&Aring;
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<StructureSection load='1lk5' size='340' side='right'caption='[[1lk5]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
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<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>
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|ACTIVITY= <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>
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</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>
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|GENE=
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<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>
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|DOMAIN=
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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=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>
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|RELATEDENTRY=[[1lk7|1LK7]]
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</table>
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1lk5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lk5 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/RPIA_PYRHO RPIA_PYRHO]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lk/1lk5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1lk5 ConSurf].
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<div style="clear:both"></div>
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'''Structure of the D-Ribose-5-Phosphate Isomerase from Pyrococcus horikoshii'''
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==See Also==
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*[[Ribose-5-phosphate isomerase 3D structures|Ribose-5-phosphate isomerase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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==About this Structure==
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1LK5 is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12057201 12057201]
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[[Category: Pyrococcus horikoshii]]
[[Category: Pyrococcus horikoshii]]
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[[Category: Ribose-5-phosphate isomerase]]
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[[Category: Cambillau C]]
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[[Category: Single protein]]
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[[Category: Ishida H]]
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[[Category: Cambillau, C.]]
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[[Category: Ishikawa K]]
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[[Category: Ishida, H.]]
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[[Category: Kawarabayasi Y]]
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[[Category: Ishikawa, K.]]
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[[Category: Kikuchi H]]
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[[Category: Kawarabayasi, Y.]]
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[[Category: Matsui I]]
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[[Category: Kikuchi, H.]]
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[[Category: Payan F]]
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[[Category: Matsui, I.]]
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[[Category: Roussel A]]
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[[Category: Payan, F.]]
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[[Category: Roussel, A.]]
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[[Category: alpha/beta structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:03:46 2008''
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Current revision

Structure of the D-Ribose-5-Phosphate Isomerase from Pyrococcus horikoshii

PDB ID 1lk5

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