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| | <StructureSection load='1r37' size='340' side='right'caption='[[1r37]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1r37' size='340' side='right'caption='[[1r37]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1r37]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R37 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1R37 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1r37]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R37 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ETX:2-ETHOXYETHANOL'>ETX</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jvb|1jvb]], [[1nto|1nto]], [[1nvg|1nvg]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ETX:2-ETHOXYETHANOL'>ETX</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADH or SSO2536 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091])</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=1r37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r37 OCA], [https://pdbe.org/1r37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r37 RCSB], [https://www.ebi.ac.uk/pdbsum/1r37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r37 ProSAT]</span></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://proteopedia.org/fgij/fg.htm?mol=1r37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r37 OCA], [http://pdbe.org/1r37 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r37 RCSB], [http://www.ebi.ac.uk/pdbsum/1r37 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r37 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ADH_SACS2 ADH_SACS2] |
| | == 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: Alcohol dehydrogenase]] | |
| - | [[Category: Atcc 35091]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bruno, I]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Esposito, L]] | + | [[Category: Bruno I]] |
| - | [[Category: Giordano, A]] | + | [[Category: Esposito L]] |
| - | [[Category: Mazzarella, L]] | + | [[Category: Giordano A]] |
| - | [[Category: Raia, C A]] | + | [[Category: Mazzarella L]] |
| - | [[Category: Rossi, M]] | + | [[Category: Raia CA]] |
| - | [[Category: Sica, F]] | + | [[Category: Rossi M]] |
| - | [[Category: Zagari, A]] | + | [[Category: Sica F]] |
| - | [[Category: Archaeon]]
| + | [[Category: Zagari A]] |
| - | [[Category: Holoform]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Zinc]]
| + | |
| Structural highlights
Function
ADH_SACS2
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
The crystal structure of a ternary complex of the alcohol dehydrogenase from the archaeon Sulfolobus solfataricus (SsADH) has been determined at 2.3 A. The asymmetric unit contains a dimer with a NADH and a 2-ethoxyethanol molecule bound to each subunit. The comparison with the apo structure of the enzyme reveals that this medium chain ADH undergoes a substantial conformational change in the apo-holo transition, accompanied by loop movements at the domain interface. The extent of domain closure is similar to that observed for the classical horse liver ADH, although some differences are found which can be related to the different oligomeric states of the enzymes. Compared to its apo form, the SsADH ternary complex shows a change in the ligation state of the active site zinc ion which is no longer bound to Glu69, providing additional evidence of the dynamic role played by the conserved glutamate residue in ADHs. In addition, the structure presented here allows the identification of the substrate site and hence of the residues that are important in the binding of both the substrate and the coenzyme.
Crystal structure of a ternary complex of the alcohol dehydrogenase from Sulfolobus solfataricus.,Esposito L, Bruno I, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A Biochemistry. 2003 Dec 16;42(49):14397-407. PMID:14661950[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Esposito L, Bruno I, Sica F, Raia CA, Giordano A, Rossi M, Mazzarella L, Zagari A. Crystal structure of a ternary complex of the alcohol dehydrogenase from Sulfolobus solfataricus. Biochemistry. 2003 Dec 16;42(49):14397-407. PMID:14661950 doi:10.1021/bi035271b
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