1k02: Difference between revisions
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==Crystal Structure of Old Yellow Enzyme Mutant Gln114Asn== | ==Crystal Structure of Old Yellow Enzyme Mutant Gln114Asn== | ||
<StructureSection load='1k02' size='340' side='right' caption='[[1k02]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='1k02' size='340' side='right' caption='[[1k02]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1oya|1oya]], [[1oyb|1oyb]], [[1oyc|1oyc]], [[1k03|1k03]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1oya|1oya]], [[1oyb|1oyb]], [[1oyc|1oyc]], [[1k03|1k03]]</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> | <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> | ||
<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=1k02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k02 OCA], [http://pdbe.org/1k02 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k02 RCSB], [http://www.ebi.ac.uk/pdbsum/1k02 PDBsum]</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=1k02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k02 OCA], [http://pdbe.org/1k02 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k02 RCSB], [http://www.ebi.ac.uk/pdbsum/1k02 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1k02 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k0/1k02_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k0/1k02_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1k02" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1k02" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:18, 17 January 2018
Crystal Structure of Old Yellow Enzyme Mutant Gln114AsnCrystal Structure of Old Yellow Enzyme Mutant Gln114Asn
Structural highlights
Function[OYE1_SACPS] Oxidizes beta-NADH, beta-NADPH, and alpha-NADPH. 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 PubMedGlutamine 114 of OYE1 is a well conserved residue in the active site of the Old Yellow Enzyme family. It forms hydrogen bonds to the O2 and N3 of the flavoprotein prosthetic group, FMN. Glutamine 114 was mutated to asparagine, introducing an R-group that is one methylene group shorter. The resultant enzyme was characterized to determine the effect of the mutation on the mechanistic behavior of the enzyme, and the crystal structure was solved to determine the effect of the mutation on the structure of the protein. The Q114N mutation results in little change in the protein structure, moving the amide group of residue 114 out of H-bonding distance, allowing repositioning of the FMN prosthetic group to form new interactions that replace the lost H-bonds. The mutation decreases the ability to bind ligands, as all dissociation constants for substituted phenols are larger than for the wild type enzyme. The rate constant for the reductive half-reaction with beta-NADPH is slightly greater, whereas that for the oxidative half-reaction with 2-cyclohexenone is smaller than for the wild type enzyme. Oxidation with molecular oxygen is biphasic and involves formation and reaction with O(2), a phenomenon that is more pronounced with this mutation than with wild type enzyme. When superoxide dismutase is added to the reaction, we observe a single-phase reaction typical of the wild type enzyme. Turnover reactions using beta-NADPH with 2-cyclohexenone and molecular oxygen were studied to further characterize the mutant enzyme. The role of glutamine 114 in old yellow enzyme.,Brown BJ, Hyun JW, Duvvuri S, Karplus PA, Massey V J Biol Chem. 2002 Jan 18;277(3):2138-45. Epub 2001 Oct 19. PMID:11668181[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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