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| | <StructureSection load='5mh4' size='340' side='right'caption='[[5mh4]], [[Resolution|resolution]] 2.14Å' scene=''> | | <StructureSection load='5mh4' size='340' side='right'caption='[[5mh4]], [[Resolution|resolution]] 2.14Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5mh4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptococcus_hollandicus"_scholl_1891 "streptococcus hollandicus" scholl 1891]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MH4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MH4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5mh4]] 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=5MH4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MH4 FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.14Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">N41_1746, NCDO763_0431 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1359 "Streptococcus hollandicus" Scholl 1891])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </span></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=5mh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mh4 OCA], [https://pdbe.org/5mh4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mh4 RCSB], [https://www.ebi.ac.uk/pdbsum/5mh4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mh4 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5mh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mh4 OCA], [http://pdbe.org/5mh4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mh4 RCSB], [http://www.ebi.ac.uk/pdbsum/5mh4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mh4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A2RLJ5_LACLM A2RLJ5_LACLM] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Streptococcus hollandicus scholl 1891]] | + | [[Category: Lactococcus cremoris]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thioredoxin-disulfide reductase]]
| + | [[Category: Bang MB]] |
| - | [[Category: Bang, M B]] | + | [[Category: Hagglund P]] |
| - | [[Category: Hagglund, P]] | + | [[Category: Harris P]] |
| - | [[Category: Harris, P]] | + | [[Category: Skjoldager N]] |
| - | [[Category: Skjoldager, N]] | + | [[Category: Svensson B]] |
| - | [[Category: Svensson, B]] | + | |
| - | [[Category: Fad si-face open space]]
| + | |
| - | [[Category: Fad-nadp+ complex]]
| + | |
| - | [[Category: Fo-fr conformation]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Oxygen pocket]]
| + | |
| - | [[Category: Photosensitivity]]
| + | |
| - | [[Category: Reactive oxygen species]]
| + | |
| - | [[Category: Thioredoxin reductase]]
| + | |
| Structural highlights
Function
A2RLJ5_LACLM
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Skjoldager N, Blanner Bang M, Rykaer M, Bjornberg O, Davies MJ, Svensson B, Harris P, Hagglund P. The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage. Sci Rep. 2017 Apr 11;7:46282. doi: 10.1038/srep46282. PMID:28397795 doi:http://dx.doi.org/10.1038/srep46282
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