1c9u

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(New page: 200px<br /><applet load="1c9u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c9u, resolution 2.20&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1c9u.gif|left|200px]]<br /><applet load="1c9u" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1c9u, resolution 2.20&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE IN COMPLEX WITH PQQ'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE IN COMPLEX WITH PQQ==
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Soluble glucose dehydrogenase (s-GDH; EC 1.1.99.17) is a classical, quinoprotein which requires the cofactor pyrroloquinoline quinone (PQQ) to, oxidize glucose to gluconolactone. The reaction mechanism of PQQ-dependent, enzymes has remained controversial due to the absence of comprehensive, structural data. We have determined the X-ray structure of s-GDH with the, cofactor at 2.2 A resolution, and of a complex with reduced PQQ and, glucose at 1.9 A resolution. These structures reveal the active site of, s-GDH, and show for the first time how a functionally bound substrate, interacts with the cofactor in a PQQ-dependent enzyme. Twenty years after, the discovery of PQQ, our results finally provide conclusive evidence for, a reaction mechanism comprising general base-catalyzed hydride transfer, rather than the generally accepted covalent addition-elimination, mechanism. Thus, PQQ-dependent enzymes use a mechanism similar to that of, nicotinamide- and flavin-dependent oxidoreductases.
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<StructureSection load='1c9u' size='340' side='right'caption='[[1c9u]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1c9u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_calcoaceticus Acinetobacter calcoaceticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C9U 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]] 2.2&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PQQ:PYRROLOQUINOLINE+QUINONE'>PQQ</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=1c9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c9u OCA], [https://pdbe.org/1c9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c9u RCSB], [https://www.ebi.ac.uk/pdbsum/1c9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c9u ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DHGB_ACICA DHGB_ACICA] Oxidizes glucose to gluconolactone.
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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/c9/1c9u_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=1c9u 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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Soluble glucose dehydrogenase (s-GDH; EC 1.1.99.17) is a classical quinoprotein which requires the cofactor pyrroloquinoline quinone (PQQ) to oxidize glucose to gluconolactone. The reaction mechanism of PQQ-dependent enzymes has remained controversial due to the absence of comprehensive structural data. We have determined the X-ray structure of s-GDH with the cofactor at 2.2 A resolution, and of a complex with reduced PQQ and glucose at 1.9 A resolution. These structures reveal the active site of s-GDH, and show for the first time how a functionally bound substrate interacts with the cofactor in a PQQ-dependent enzyme. Twenty years after the discovery of PQQ, our results finally provide conclusive evidence for a reaction mechanism comprising general base-catalyzed hydride transfer, rather than the generally accepted covalent addition-elimination mechanism. Thus, PQQ-dependent enzymes use a mechanism similar to that of nicotinamide- and flavin-dependent oxidoreductases.
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==About this Structure==
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Structure and mechanism of soluble quinoprotein glucose dehydrogenase.,Oubrie A, Rozeboom HJ, Kalk KH, Olsthoorn AJ, Duine JA, Dijkstra BW EMBO J. 1999 Oct 1;18(19):5187-94. PMID:10508152<ref>PMID:10508152</ref>
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1C9U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acinetobacter_calcoaceticus Acinetobacter calcoaceticus] with CA, PQQ and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Quinoprotein_glucose_dehydrogenase Quinoprotein glucose dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.5.2 1.1.5.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C9U 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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Structure and mechanism of soluble quinoprotein glucose dehydrogenase., Oubrie A, Rozeboom HJ, Kalk KH, Olsthoorn AJ, Duine JA, Dijkstra BW, EMBO J. 1999 Oct 1;18(19):5187-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10508152 10508152]
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</div>
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<div class="pdbe-citations 1c9u" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Acinetobacter calcoaceticus]]
[[Category: Acinetobacter calcoaceticus]]
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[[Category: Quinoprotein glucose dehydrogenase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Dijkstra BW]]
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[[Category: Dijkstra, B.W.]]
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[[Category: Oubrie A]]
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[[Category: Oubrie, A.]]
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[[Category: Rozeboom HJ]]
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[[Category: Rozeboom, H.J.]]
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[[Category: CA]]
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[[Category: GOL]]
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[[Category: PQQ]]
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[[Category: beta-propeller]]
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[[Category: cofactor binding]]
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[[Category: superbarrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:17:41 2007''
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Current revision

CRYSTAL STRUCTURE OF THE SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE IN COMPLEX WITH PQQ

PDB ID 1c9u

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