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| | <StructureSection load='4cvc' size='340' side='right'caption='[[4cvc]], [[Resolution|resolution]] 1.83Å' scene=''> | | <StructureSection load='4cvc' size='340' side='right'caption='[[4cvc]], [[Resolution|resolution]] 1.83Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cvc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"pseudogluconobacter_saccharoketogenes"_shibata_et_al._2001 "pseudogluconobacter saccharoketogenes" shibata et al. 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CVC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cvc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudogluconobacter_saccharoketogenes Pseudogluconobacter saccharoketogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CVC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PPI:PROPANOIC+ACID'>PPI</scene>, <scene name='pdbligand=PQQ:PYRROLOQUINOLINE+QUINONE'>PQQ</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.83Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cvb|4cvb]]</td></tr>
| + | <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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PPI:PROPANOIC+ACID'>PPI</scene>, <scene name='pdbligand=PQQ:PYRROLOQUINOLINE+QUINONE'>PQQ</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(cytochrome_c) Alcohol dehydrogenase (cytochrome c)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.2.8 1.1.2.8] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4cvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cvc OCA], [https://pdbe.org/4cvc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cvc RCSB], [https://www.ebi.ac.uk/pdbsum/4cvc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cvc ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cvc OCA], [http://pdbe.org/4cvc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cvc RCSB], [http://www.ebi.ac.uk/pdbsum/4cvc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cvc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q93RE9_9BACT Q93RE9_9BACT] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pseudogluconobacter saccharoketogenes shibata et al. 2001]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dijkstra, B W]] | + | [[Category: Pseudogluconobacter saccharoketogenes]] |
| - | [[Category: Mikkelsen, R]] | + | [[Category: Dijkstra BW]] |
| - | [[Category: Mulder, H]] | + | [[Category: Mikkelsen R]] |
| - | [[Category: Nikolaev, I]] | + | [[Category: Mulder H]] |
| - | [[Category: Rozeboom, H J]] | + | [[Category: Nikolaev I]] |
| - | [[Category: Yu, S]] | + | [[Category: Rozeboom HJ]] |
| - | [[Category: Carbohydrate oxidation]]
| + | [[Category: Yu S]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Quinoprotein]]
| + | |
| Structural highlights
4cvc is a 1 chain structure with sequence from Pseudogluconobacter saccharoketogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.83Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q93RE9_9BACT
Publication Abstract from PubMed
The quinone-dependent alcohol dehydrogenase (PQQ-ADH, E.C. 1.1.5.2) from the Gram-negative bacterium Pseudogluconobacter saccharoketogenes IFO 14464 oxidizes primary alcohols (e.g. ethanol, butanol), secondary alcohols (monosaccharides), as well as aldehydes, polysaccharides, and cyclodextrins. The recombinant protein, expressed in Pichia pastoris, was crystallized, and three-dimensional (3D) structures of the native form, with PQQ and a Ca2+ ion, and of the enzyme in complex with a Zn2+ ion and a bound substrate mimic were determined at 1.72 A and 1.84 A resolution, respectively. PQQ-ADH displays an eight-bladed beta-propeller fold, characteristic of Type I quinone-dependent methanol dehydrogenases. However, three of the four ligands of the Ca2+ ion differ from those of related dehydrogenases and they come from different parts of the polypeptide chain. These differences result in a more open, easily accessible active site, which explains why PQQ-ADH can oxidize a broad range of substrates. The bound substrate mimic suggests Asp333 as the catalytic base. Remarkably, no vicinal disulfide bridge is present near the PQQ, which in other PQQ-dependent alcohol dehydrogenases has been proposed to be necessary for electron transfer. Instead an associated cytochrome c can approach the PQQ for direct electron transfer.
Crystal structure of quinone-dependent alcohol dehydrogenase from Pseudogluconobacter saccharoketogenes. A versatile dehydrogenase oxidizing alcohols and carbohydrates.,Rozeboom HJ, Yu S, Mikkelsen R, Nikolaev I, Mulder HJ, Dijkstra BW Protein Sci. 2015 Oct 6. doi: 10.1002/pro.2818. PMID:26440996[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rozeboom HJ, Yu S, Mikkelsen R, Nikolaev I, Mulder HJ, Dijkstra BW. Crystal structure of quinone-dependent alcohol dehydrogenase from Pseudogluconobacter saccharoketogenes. A versatile dehydrogenase oxidizing alcohols and carbohydrates. Protein Sci. 2015 Oct 6. doi: 10.1002/pro.2818. PMID:26440996 doi:http://dx.doi.org/10.1002/pro.2818
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