1lk7

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(New page: 200px<br /><applet load="1lk7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lk7, resolution 2.0&Aring;" /> '''Structure of D-Ribose...)
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[[Image:1lk7.jpg|left|200px]]<br /><applet load="1lk7" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lk7, resolution 2.0&Aring;" />
 
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'''Structure of D-Ribose-5-Phosphate Isomerase from in complex with phospho-erythronic acid'''<br />
 
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==Overview==
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==Structure of D-Ribose-5-Phosphate Isomerase from in complex with phospho-erythronic acid==
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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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<StructureSection load='1lk7' size='340' side='right'caption='[[1lk7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1lk7]] 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=1LK7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LK7 FirstGlance]. <br>
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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]] 2&#8491;</td></tr>
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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=DER:D-4-PHOSPHOERYTHRONIC+ACID'>DER</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=1lk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lk7 OCA], [https://pdbe.org/1lk7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lk7 RCSB], [https://www.ebi.ac.uk/pdbsum/1lk7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lk7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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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/1lk7_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=1lk7 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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==About this Structure==
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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:12057201<ref>PMID:12057201</ref>
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1LK7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with CL, NA and DER as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LK7 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12057201 12057201]
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</div>
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[[Category: Pyrococcus horikoshii]]
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<div class="pdbe-citations 1lk7" style="background-color:#fffaf0;"></div>
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[[Category: Ribose-5-phosphate isomerase]]
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[[Category: Single protein]]
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[[Category: Cambillau, C.]]
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[[Category: Ishida, H.]]
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[[Category: Ishikawa, K.]]
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[[Category: Kawarabayasi, Y.]]
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[[Category: Kikuchi, H.]]
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[[Category: Matsui, I.]]
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[[Category: Payan, F.]]
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[[Category: Roussel, A.]]
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[[Category: CL]]
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[[Category: DER]]
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[[Category: NA]]
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[[Category: alpha/beta structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:37:12 2007''
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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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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pyrococcus horikoshii]]
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[[Category: Cambillau C]]
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[[Category: Ishida H]]
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[[Category: Ishikawa K]]
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[[Category: Kawarabayasi Y]]
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[[Category: Kikuchi H]]
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[[Category: Matsui I]]
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[[Category: Payan F]]
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[[Category: Roussel A]]

Current revision

Structure of D-Ribose-5-Phosphate Isomerase from in complex with phospho-erythronic acid

PDB ID 1lk7

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