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| | ==1.75A resolution structure of a thermostable alcohol dehydrogenase from Pyrobaculum aerophilum== | | ==1.75A resolution structure of a thermostable alcohol dehydrogenase from Pyrobaculum aerophilum== |
| - | <StructureSection load='4jbg' size='340' side='right' caption='[[4jbg]], [[Resolution|resolution]] 1.75Å' scene=''> | + | <StructureSection load='4jbg' size='340' side='right'caption='[[4jbg]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4jbg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrae Pyrae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JBG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JBG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4jbg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_aerophilum_str._IM2 Pyrobaculum aerophilum str. IM2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JBG 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=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </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=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jbh|4jbh]], [[4jbi|4jbi]], [[4jbu|4jbu]]</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=4jbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jbg OCA], [https://pdbe.org/4jbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jbg RCSB], [https://www.ebi.ac.uk/pdbsum/4jbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jbg ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAE2687 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=178306 PYRAE])</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 Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] </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=4jbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jbg OCA], [http://pdbe.org/4jbg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jbg RCSB], [http://www.ebi.ac.uk/pdbsum/4jbg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jbg ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8ZUP0_PYRAE Q8ZUP0_PYRAE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4jbg" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4jbg" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alcohol dehydrogenase]] | + | [[Category: Large Structures]] |
| - | [[Category: Pyrae]] | + | [[Category: Pyrobaculum aerophilum str. IM2]] |
| - | [[Category: Auld, D S]] | + | [[Category: Auld DS]] |
| - | [[Category: Auria, S D]] | + | [[Category: Battaile KP]] |
| - | [[Category: Battaile, K P]] | + | [[Category: D'Auria S]] |
| - | [[Category: Hu, X]] | + | [[Category: Hu X]] |
| - | [[Category: Lovell, S]] | + | [[Category: Lovell S]] |
| - | [[Category: Shen, M]] | + | [[Category: Shen M]] |
| - | [[Category: Throne, N]] | + | [[Category: Throne N]] |
| - | [[Category: Vitale, A]] | + | [[Category: Vitale A]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Thermostability]]
| + | |
| - | [[Category: Zinc binding]]
| + | |
| Structural highlights
Function
Q8ZUP0_PYRAE
Publication Abstract from PubMed
In this work we characterize an alcohol dehydrogenase (ADH) from the hyperthermophilic archaeon Pyrobaculum aerophilum (PyAeADHII). We have previously found that PyAeADHII has no activity when standard ADH substrates are used but is active when alpha-tetralone is used as substrate. Here, to gain insights into enzyme function, we screened several chemical libraries for enzymatic modulators using an assay employing alpha-tetralone. The results indicate that PyAeADHII activity in the presence of alpha-tetralone was inhibited by compounds such as flunarizine. We also examined metal coordination of the enzyme in solution by performing metal substitution of the enzyme-bound zinc (Zn(2+)) with cobalt. The solution-based absorption spectra for cobalt substituted PyAeADHII supports substitution at the structural Zn(2+) site. To gain structural insight, we obtained the crystal structure of both wild-type and cobalt-substituted PyAeADHII at 1.75 A and 2.20 A resolution, respectively. The X-ray data confirmed one metal ion per monomer present only at the structural site with otherwise close conservation to other ADH enzymes. We next determined the co-crystal structure of the NADPH-bound form of the enzyme at 2.35 A resolution to help define the active site region of the enzyme and this data shows close structural conservation with horse ADH, despite the lack of a catalytic Zn(2+) ion in PyAeADHII. Modeling of alpha-tetralone into the NADPH bound structure suggests an arginine as a possible catalytic residue. The data presented here can yield a better understanding of alcohol dehydrogenases lacking the catalytic zinc as well as the structural features inherent to thermostable enzymes.
Physicochemical Characterization of a Thermostable Alcohol Dehydrogenase from Pyrobaculum aerophilum.,Vitale A, Thorne N, Lovell S, Battaile KP, Hu X, Shen M, D'Auria S, Auld DS PLoS One. 2013 Jun 5;8(6):e63828. doi: 10.1371/journal.pone.0063828. Print 2013. PMID:23755111[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Vitale A, Thorne N, Lovell S, Battaile KP, Hu X, Shen M, D'Auria S, Auld DS. Physicochemical Characterization of a Thermostable Alcohol Dehydrogenase from Pyrobaculum aerophilum. PLoS One. 2013 Jun 5;8(6):e63828. doi: 10.1371/journal.pone.0063828. Print 2013. PMID:23755111 doi:10.1371/journal.pone.0063828
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