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| ==Old Yellow Enzyme from Thermus scotoductus SA-01== | | ==Old Yellow Enzyme from Thermus scotoductus SA-01== |
| <StructureSection load='3hf3' size='340' side='right' caption='[[3hf3]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='3hf3' size='340' side='right'caption='[[3hf3]], [[Resolution|resolution]] 2.20Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3hf3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51532 Atcc 51532]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HF3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HF3 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3hf3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_scotoductus Thermus scotoductus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HF3 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.2Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hgj|3hgj]]</td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CrS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=37636 ATCC 51532])</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=3hf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hf3 OCA], [https://pdbe.org/3hf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hf3 RCSB], [https://www.ebi.ac.uk/pdbsum/3hf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hf3 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/NADPH_dehydrogenase NADPH dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.99.1 1.6.99.1] </span></td></tr>
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| <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=3hf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hf3 OCA], [http://pdbe.org/3hf3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hf3 RCSB], [http://www.ebi.ac.uk/pdbsum/3hf3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hf3 ProSAT]</span></td></tr> | |
| </table> | | </table> |
| | == Function == |
| | [https://www.uniprot.org/uniprot/B0JDW3_THESC B0JDW3_THESC] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hf3 ConSurf]. | | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hf3 ConSurf]. |
| <div style="clear:both"></div> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Recent characterization of the chromate reductase (CrS) from the thermophile Thermus scotoductus SA-01 revealed this enzyme to be related to the Old Yellow Enzyme (OYE) family. Here, we report the structure of a thermostable OYE homolog in its holoform at 2.2A as well as its complex with p-hydroxybenzaldehyde (pHBA). The enzyme crystallized as octamers with the monomers showing a classical TIM barrel fold which upon dimerization yields the biologically active form of the protein. A sulfate ion is bound above the si-side of the non-covalently bound FMN cofactor in the oxidized solved structure but is displaced upon pHBA binding. The active-site architecture is highly conserved as with other members of this enzyme family. The pHBA in the CrS complex is positioned by hydrogen bonding to the two conserved catalytic-site histidines. The most prominent structural difference between CrS and other OYE homologs is the size of the "capping domain". Thermostabilization of the enzyme is achieved in part through increased proline content within loops and turns as well as increased intersubunit interactions through hydrogen bonding and complex salt bridge networks. CrS is able to reduce the C=C bonds of alpha,beta-unsaturated carbonyl compounds with a preference towards cyclic substrates however no activity was observed towards beta-substituted substrates. Mutational studies have confirmed the role of Tyr177 as the proposed proton donor although reduction could still occur at a reduced rate when this residue was mutated to phenylalanine.
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| Crystal structure of a thermostable old yellow enzyme from Thermus scotoductus SA-01.,Opperman DJ, Sewell BT, Litthauer D, Isupov MN, Littlechild JA, van Heerden E Biochem Biophys Res Commun. 2010 Mar 12;393(3):426-31. Epub 2010 Feb 6. PMID:20138824<ref>PMID:20138824</ref>
| | ==See Also== |
| | | *[[NADPH dehydrogenase|NADPH dehydrogenase]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3hf3" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Atcc 51532]] | | [[Category: Large Structures]] |
| [[Category: NADPH dehydrogenase]] | | [[Category: Thermus scotoductus]] |
| [[Category: Heerden, E van]]
| | [[Category: Isupov MN]] |
| [[Category: Isupov, M N]] | | [[Category: Litthauer D]] |
| [[Category: Litthauer, D]] | | [[Category: Littlechild JA]] |
| [[Category: Littlechild, J A]] | | [[Category: Opperman DJ]] |
| [[Category: Opperman, D J]] | | [[Category: Sewell BT]] |
| [[Category: Sewell, B T]] | | [[Category: Van Heerden E]] |
| [[Category: Oxidoreductase]] | |
| [[Category: Tim barrel]]
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