1o9b

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{{Seed}}
 
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[[Image:1o9b.png|left|200px]]
 
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==QUINATE/SHIKIMATE DEHYDROGENASE YDIB COMPLEXED WITH NADH==
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The line below this paragraph, containing "STRUCTURE_1o9b", creates the "Structure Box" on the page.
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<StructureSection load='1o9b' size='340' side='right'caption='[[1o9b]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1o9b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O9B FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.5&#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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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{{STRUCTURE_1o9b| PDB=1o9b | SCENE= }}
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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=1o9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o9b OCA], [https://pdbe.org/1o9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o9b RCSB], [https://www.ebi.ac.uk/pdbsum/1o9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o9b ProSAT], [https://www.topsan.org/Proteins/BSGI/1o9b TOPSAN]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/YDIB_ECOLI YDIB_ECOLI] The physiological substrate is not known.<ref>PMID:12624088</ref>
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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/o9/1o9b_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1o9b 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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Shikimate dehydrogenase catalyzes the fourth step of the shikimate pathway, the essential route for the biosynthesis of aromatic compounds in plants and microorganisms. Absent in metazoans, this pathway is an attractive target for nontoxic herbicides and drugs. Escherichia coli expresses two shikimate dehydrogenase paralogs, the NADP-specific AroE and a putative enzyme YdiB. Here we characterize YdiB as a dual specificity quinate/shikimate dehydrogenase that utilizes either NAD or NADP as a cofactor. Structures of AroE and YdiB with bound cofactors were determined at 1.5 and 2.5 A resolution, respectively. Both enzymes display a similar architecture with two alpha/beta domains separated by a wide cleft. Comparison of their dinucleotide-binding domains reveals the molecular basis for cofactor specificity. Independent molecules display conformational flexibility suggesting that a switch between open and closed conformations occurs upon substrate binding. Sequence analysis and structural comparison led us to propose the catalytic machinery and a model for 3-dehydroshikimate recognition. Furthermore, we discuss the evolutionary and metabolic implications of the presence of two shikimate dehydrogenases in E. coli and other organisms.
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===QUINATE/SHIKIMATE DEHYDROGENASE YDIB COMPLEXED WITH NADH===
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Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities.,Michel G, Roszak AW, Sauve V, Maclean J, Matte A, Coggins JR, Cygler M, Lapthorn AJ J Biol Chem. 2003 May 23;278(21):19463-72. Epub 2003 Mar 12. PMID:12637497<ref>PMID:12637497</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_12637497}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1o9b" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12637497 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12637497}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1O9B is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O9B OCA].
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==Reference==
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<ref group="xtra">PMID:12637497</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Shikimate dehydrogenase]]
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[[Category: Large Structures]]
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[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
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[[Category: Cygler M]]
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[[Category: Cygler, M.]]
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[[Category: Michel G]]
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[[Category: Michel, G.]]
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[[Category: Bsgi]]
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[[Category: Montreal-kingston bacterial structural genomics initiative]]
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[[Category: Nad]]
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[[Category: Oxidoreductase]]
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[[Category: Quinate]]
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[[Category: Shikimate]]
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[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 11:51:50 2009''
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Current revision

QUINATE/SHIKIMATE DEHYDROGENASE YDIB COMPLEXED WITH NADH

PDB ID 1o9b

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