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| | <StructureSection load='3a9h' size='340' side='right'caption='[[3a9h]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='3a9h' size='340' side='right'caption='[[3a9h]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3a9h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51768 Atcc 51768]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A9H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A9H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3a9h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A9H FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PQQ:PYRROLOQUINOLINE+QUINONE'>PQQ</scene>, <scene name='pdbligand=TRE:TREHALOSE'>TRE</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]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a9g|3a9g]]</td></tr> | + | <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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PQQ:PYRROLOQUINOLINE+QUINONE'>PQQ</scene>, <scene name='pdbligand=PRD_900006:trehalose'>PRD_900006</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Quinoprotein_glucose_dehydrogenase_(PQQ,_quinone) Quinoprotein glucose dehydrogenase (PQQ, quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.5.2 1.1.5.2] </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=3a9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a9h OCA], [https://pdbe.org/3a9h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a9h RCSB], [https://www.ebi.ac.uk/pdbsum/3a9h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a9h 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=3a9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a9h OCA], [http://pdbe.org/3a9h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a9h RCSB], [http://www.ebi.ac.uk/pdbsum/3a9h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a9h ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8ZUN8_PYRAE Q8ZUN8_PYRAE] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 51768]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ohshima, T]] | + | [[Category: Pyrobaculum aerophilum]] |
| - | [[Category: Sakuraba, H]] | + | [[Category: Ohshima T]] |
| - | [[Category: Yokono, K]] | + | [[Category: Sakuraba H]] |
| - | [[Category: Yoneda, K]] | + | [[Category: Yokono K]] |
| - | [[Category: Aldose sugar dehydrogenase]]
| + | [[Category: Yoneda K]] |
| - | [[Category: Beta-propeller fold]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Pqq dependent dehydrogenase]]
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| Structural highlights
Function
Q8ZUN8_PYRAE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
We identified a gene encoding a soluble quinoprotein glucose dehydrogenase homologue in the hyperthermophilic archaeon Pyrobaculum aerophilum. The gene was overexpressed in Escherichia coli, after which its product was purified and characterized. The enzyme was extremely thermostable, and the activity of the pyrroloquinoline quinone (PQQ)-bound holoenzyme was not lost after incubation at 100 degrees C for 10min. The crystal structure of the enzyme was determined in both the apoform and as the PQQ-bound holoenzyme. The overall fold of the P. aerophilum enzyme showed significant similarity to that of soluble quinoprotein aldose sugar dehydrogenase (Asd) from E. coli. However, clear topological differences were observed in the two long loops around the PQQ-binding sites of the two enzymes. Structural comparison revealed that the hyperthermostability of the P. aerophilum enzyme is likely attributable to the presence of an extensive aromatic pair network located around a beta-sheet involving N- and C-terminal beta-strands.
Catalytic properties and crystal structure of quinoprotein aldose sugar dehydrogenase from hyperthermophilic archaeon Pyrobaculum aerophilum.,Sakuraba H, Yokono K, Yoneda K, Watanabe A, Asada Y, Satomura T, Yabutani T, Motonaka J, Ohshima T Arch Biochem Biophys. 2010 Oct 15;502(2):81-8. Epub 2010 Aug 6. PMID:20692227[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sakuraba H, Yokono K, Yoneda K, Watanabe A, Asada Y, Satomura T, Yabutani T, Motonaka J, Ohshima T. Catalytic properties and crystal structure of quinoprotein aldose sugar dehydrogenase from hyperthermophilic archaeon Pyrobaculum aerophilum. Arch Biochem Biophys. 2010 Oct 15;502(2):81-8. Epub 2010 Aug 6. PMID:20692227 doi:10.1016/j.abb.2010.08.002
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