3hf3: Difference between revisions
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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 [ | <table><tr><td colspan='2'>[[3hf3]] is a 4 chain structure with sequence from [https://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 [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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hgj|3hgj]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hgj|3hgj]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CrS ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CrS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=37636 ATCC 51532])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NADPH_dehydrogenase NADPH dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.99.1 1.6.99.1] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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</div> | </div> | ||
<div class="pdbe-citations 3hf3" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3hf3" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[NADPH dehydrogenase|NADPH dehydrogenase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 51532]] | [[Category: Atcc 51532]] | ||
[[Category: Large Structures]] | |||
[[Category: NADPH dehydrogenase]] | [[Category: NADPH dehydrogenase]] | ||
[[Category: Heerden, E van]] | [[Category: Heerden, E van]] | ||
Revision as of 15:46, 23 March 2022
Old Yellow Enzyme from Thermus scotoductus SA-01Old Yellow Enzyme from Thermus scotoductus SA-01
Structural highlights
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 PubMedRecent 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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