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1cru

From Proteopedia

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[[Image:1cru.gif|left|200px]]<br /><applet load="1cru" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cru, resolution 1.50&Aring;" />
 
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'''SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CALCOACETICUS IN COMPLEX WITH PQQ AND METHYLHYDRAZINE'''<br />
 
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==Overview==
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==SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CALCOACETICUS IN COMPLEX WITH PQQ AND METHYLHYDRAZINE==
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Soluble glucose dehydrogenase (s-GDH) from the bacterium Acinetobacter calcoaceticus is a classical quinoprotein. It requires the cofactor pyrroloquinoline quinone (PQQ) to catalyze the oxidation of glucose to gluconolactone. The precise catalytic role of PQQ in s-GDH and several other PQQ-dependent enzymes has remained controversial because of the absence of comprehensive structural data. We have determined the crystal structure of a ternary complex of s-GDH with PQQ and methylhydrazine, a competitive inhibitor of the enzyme. This complex, refined at 1.5-A resolution to an R factor of 16.7%, affords a detailed view of a cofactor-binding site of s-GDH. Moreover, it presents the first direct observation of covalent PQQ adduct in the active-site of a PQQ-dependent enzyme, thereby confirming previous evidence that the C5 carbonyl group of the cofactor is the most reactive moiety of PQQ.
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<StructureSection load='1cru' size='340' side='right'caption='[[1cru]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1cru]] 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=1CRU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CRU FirstGlance]. <br>
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1CRU 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 <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=PQQ:'>PQQ</scene>, <scene name='pdbligand=PQQ:'>PQQ</scene>, <scene name='pdbligand=HDN:'>HDN</scene> and <scene name='pdbligand=GOL:'>GOL</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1CRU OCA].
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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]] 1.5&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HDN:METHYLHYDRAZINE'>HDN</scene>, <scene name='pdbligand=PQQ:PYRROLOQUINOLINE+QUINONE'>PQQ</scene></td></tr>
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==Reference==
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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=1cru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cru OCA], [https://pdbe.org/1cru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cru RCSB], [https://www.ebi.ac.uk/pdbsum/1cru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cru ProSAT]</span></td></tr>
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Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: a covalent cofactor-inhibitor complex., Oubrie A, Rozeboom HJ, Dijkstra BW, Proc Natl Acad Sci U S A. 1999 Oct 12;96(21):11787-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10518528 10518528]
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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/cr/1cru_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=1cru ConSurf].
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<div style="clear:both"></div>
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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: HDN]]
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[[Category: PQQ]]
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[[Category: beta-propeller]]
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[[Category: complex with the cofactor pqq and the inhibitor methylhydrazine]]
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[[Category: oxidoreductase]]
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[[Category: superbarrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:09:08 2008''
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Current revision

SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CALCOACETICUS IN COMPLEX WITH PQQ AND METHYLHYDRAZINE

PDB ID 1cru

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