5mjk: Difference between revisions
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==Crystal Structure of Lactococcus lactis Thioredoxin Reductase (FO conformation)== | |||
<StructureSection load='5mjk' size='340' side='right'caption='[[5mjk]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5mjk]] is a 4 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=5MJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MJK FirstGlance]. <br> | |||
</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=SO4:SULFATE+ION'>SO4</scene></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=5mjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mjk OCA], [https://pdbe.org/5mjk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mjk RCSB], [https://www.ebi.ac.uk/pdbsum/5mjk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mjk ProSAT]</span></td></tr> | |||
</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> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5mjk" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]] | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lactococcus cremoris]] | |||
[[Category: Large Structures]] | |||
[[Category: Bang MB]] | |||
[[Category: Hagglund P]] | |||
[[Category: Harris P]] | |||
[[Category: Skjoldager N]] | |||
[[Category: Svensson B]] | |||
Latest revision as of 21:46, 1 November 2023
Crystal Structure of Lactococcus lactis Thioredoxin Reductase (FO conformation)Crystal Structure of Lactococcus lactis Thioredoxin Reductase (FO conformation)
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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