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| | <StructureSection load='2zk7' size='340' side='right'caption='[[2zk7]], [[Resolution|resolution]] 2.71Å' scene=''> | | <StructureSection load='2zk7' size='340' side='right'caption='[[2zk7]], [[Resolution|resolution]] 2.71Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2zk7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZK7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZK7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2zk7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZK7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZK7 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2dtd|2dtd]], [[2dte|2dte]], [[2dtx|2dtx]]</div></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]] 2.71Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ta0754 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glucose_1-dehydrogenase_(NAD(+)) Glucose 1-dehydrogenase (NAD(+))], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.118 1.1.1.118] </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=2zk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zk7 OCA], [https://pdbe.org/2zk7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zk7 RCSB], [https://www.ebi.ac.uk/pdbsum/2zk7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zk7 ProSAT]</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=2zk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zk7 OCA], [https://pdbe.org/2zk7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zk7 RCSB], [https://www.ebi.ac.uk/pdbsum/2zk7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zk7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9HK51_THEAC Q9HK51_THEAC] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nishioka, T]] | + | [[Category: Thermoplasma acidophilum]] |
| - | [[Category: Nishiya, Y]] | + | [[Category: Nishioka T]] |
| - | [[Category: Tamura, N]] | + | [[Category: Nishiya Y]] |
| - | [[Category: Tamura, T]] | + | [[Category: Tamura N]] |
| - | [[Category: Yasutake, Y]] | + | [[Category: Tamura T]] |
| - | [[Category: Oxidoreductase]]
| + | [[Category: Yasutake Y]] |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
Q9HK51_THEAC
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 D-aldohexose dehydrogenase from the thermoacidophilic archaeon Thermoplasma acidophilum (AldT) is a homotetrameric enzyme that catalyzes the oxidation of several D-aldohexoses, especially D-mannose. AldT comprises a unique C-terminal tail motif (residues 247-255) that shuts the active-site pocket of the neighboring subunit. The functional role of the C-terminal tail of AldT has been investigated using mutational and crystallographic analyses. A total of four C-terminal deletion mutants (Delta254, Delta253, Delta252, and Delta249) and two site-specific mutants (Y86G and P254G) were expressed by Escherichia coli and purified. Enzymatic characterization of these mutants revealed that the C-terminal tail is a requisite and that the interaction between Tyr86 and Pro254 is critical for enzyme activity. The crystal structure of the Delta249 mutant was also determined. The structure showed that the active-site loops undergo a significant conformational change, which leads to the structural deformation of the substrate-binding pocket. Proteins 2009. (c) 2008 Wiley-Liss, Inc.
C-terminal tail derived from the neighboring subunit is critical for the activity of Thermoplasma acidophilumD-aldohexose dehydrogenase.,Nishioka T, Yasutake Y, Nishiya Y, Tamura N, Tamura T Proteins. 2008 Oct 21. PMID:19089950[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nishioka T, Yasutake Y, Nishiya Y, Tamura N, Tamura T. C-terminal tail derived from the neighboring subunit is critical for the activity of Thermoplasma acidophilumD-aldohexose dehydrogenase. Proteins. 2008 Oct 21. PMID:19089950 doi:http://dx.doi.org/10.1002/prot.22300
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