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==Crystal Structure of Lactococcus lactis Thioredoxin Reductase Exposed to Visible Light (120 min)== | ==Crystal Structure of Lactococcus lactis Thioredoxin Reductase Exposed to Visible Light (120 min)== | ||
<StructureSection load='5mir' size='340' side='right' caption='[[5mir]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='5mir' size='340' side='right'caption='[[5mir]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5mir]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MIR OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5mir]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_cremoris Lactococcus cremoris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MIR FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5mir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mir OCA], [https://pdbe.org/5mir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mir RCSB], [https://www.ebi.ac.uk/pdbsum/5mir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mir ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A2RLJ5_LACLM A2RLJ5_LACLM] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The NADPH-dependent homodimeric flavoenzyme thioredoxin reductase (TrxR) provides reducing equivalents to thioredoxin, a key regulator of various cellular redox processes. Crystal structures of photo-inactivated thioredoxin reductase (TrxR) from the Gram-positive bacterium Lactococcus lactis have been determined. These structures reveal novel molecular features that provide further insight into the mechanisms behind the sensitivity of this enzyme toward visible light. We propose that a pocket on the si-face of the isoalloxazine ring accommodates oxygen that reacts with photo-excited FAD generating superoxide and a flavin radical that oxidize the isoalloxazine ring C7alpha methyl group and a nearby tyrosine residue. This tyrosine and key residues surrounding the oxygen pocket are conserved in enzymes from related bacteria, including pathogens such as Staphylococcus aureus. Photo-sensitivity may thus be a widespread feature among bacterial TrxR with the described characteristics, which affords applications in clinical photo-therapy of drug-resistant bacteria. | |||
The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage.,Skjoldager N, Blanner Bang M, Rykaer M, Bjornberg O, Davies MJ, Svensson B, Harris P, Hagglund P Sci Rep. 2017 Apr 11;7:46282. doi: 10.1038/srep46282. PMID:28397795<ref>PMID:28397795</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5mir" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Lactococcus cremoris]] | ||
[[Category: Bang | [[Category: Large Structures]] | ||
[[Category: Hagglund | [[Category: Bang MB]] | ||
[[Category: Harris | [[Category: Hagglund P]] | ||
[[Category: Skjoldager | [[Category: Harris P]] | ||
[[Category: Svensson | [[Category: Skjoldager N]] | ||
[[Category: Svensson B]] | |||
Latest revision as of 21:45, 1 November 2023
Crystal Structure of Lactococcus lactis Thioredoxin Reductase Exposed to Visible Light (120 min)Crystal Structure of Lactococcus lactis Thioredoxin Reductase Exposed to Visible Light (120 min)
Structural highlights
FunctionPublication Abstract from PubMedThe NADPH-dependent homodimeric flavoenzyme thioredoxin reductase (TrxR) provides reducing equivalents to thioredoxin, a key regulator of various cellular redox processes. Crystal structures of photo-inactivated thioredoxin reductase (TrxR) from the Gram-positive bacterium Lactococcus lactis have been determined. These structures reveal novel molecular features that provide further insight into the mechanisms behind the sensitivity of this enzyme toward visible light. We propose that a pocket on the si-face of the isoalloxazine ring accommodates oxygen that reacts with photo-excited FAD generating superoxide and a flavin radical that oxidize the isoalloxazine ring C7alpha methyl group and a nearby tyrosine residue. This tyrosine and key residues surrounding the oxygen pocket are conserved in enzymes from related bacteria, including pathogens such as Staphylococcus aureus. Photo-sensitivity may thus be a widespread feature among bacterial TrxR with the described characteristics, which affords applications in clinical photo-therapy of drug-resistant bacteria. The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage.,Skjoldager N, Blanner Bang M, Rykaer M, Bjornberg O, Davies MJ, Svensson B, Harris P, Hagglund P Sci Rep. 2017 Apr 11;7:46282. doi: 10.1038/srep46282. PMID:28397795[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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