1cq1

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(New page: 200px<br /> <applet load="1cq1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cq1, resolution 1.9&Aring;" /> '''SOLUBLE QUINOPROTEIN...)
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[[Image:1cq1.gif|left|200px]]<br />
 
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<applet load="1cq1" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cq1, resolution 1.9&Aring;" />
 
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'''SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CALCOACETICUS IN COMPLEX WITH PQQH2 AND GLUCOSE'''<br />
 
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==Overview==
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==Soluble Quinoprotein Glucose Dehydrogenase from Acinetobacter Calcoaceticus in Complex with PQQH2 and Glucose==
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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='1cq1' size='340' side='right'caption='[[1cq1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cq1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_calcoaceticus Acinetobacter calcoaceticus]. The May 2006 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Glucose Oxidase'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2006_5 10.2210/rcsb_pdb/mom_2006_5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CQ1 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]] 1.9&#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=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1cq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cq1 OCA], [https://pdbe.org/1cq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cq1 RCSB], [https://www.ebi.ac.uk/pdbsum/1cq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cq1 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/cq/1cq1_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=1cq1 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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1CQ1 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 GLC, CA and PQQ as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1CQ1 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb77_1.html Glucose Oxidase]]. 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=1CQ1 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 1cq1" 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]]
[[Category: Glucose Oxidase]]
[[Category: Glucose Oxidase]]
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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: RCSB PDB Molecule of the Month]]
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[[Category: Dijkstra, B.W.]]
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[[Category: Dijkstra BW]]
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[[Category: Oubrie, A.]]
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[[Category: Oubrie A]]
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[[Category: Rozeboom, H.J.]]
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[[Category: Rozeboom HJ]]
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[[Category: CA]]
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[[Category: GLC]]
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[[Category: PQQ]]
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[[Category: beta-propeller]]
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[[Category: complex with cofactor and substrate]]
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[[Category: superbarrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 08:58:32 2007''
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Current revision

Soluble Quinoprotein Glucose Dehydrogenase from Acinetobacter Calcoaceticus in Complex with PQQH2 and Glucose

PDB ID 1cq1

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