5MIS
Crystal Structure of Lactococcus lactis Thioredoxin Reductase Exposed to Visible Light (180 min)
Summary for 5MIS
| Entry DOI | 10.2210/pdb5mis/pdb |
| Descriptor | Thioredoxin reductase, FLAVIN-ADENINE DINUCLEOTIDE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (6 entities in total) |
| Functional Keywords | thioredoxin reductase, photosensitivity, reactive oxygen species, fad si-face open space, oxygen pocket, fad-nadp+ complex, fo-fr conformations, oxidoreductase |
| Biological source | Lactococcus lactis subsp. cremoris |
| Total number of polymer chains | 1 |
| Total formula weight | 37959.93 |
| Authors | Skjoldager, N.,Bang, M.B.,Svensson, B.,Hagglund, P.,Harris, P. (deposition date: 2016-11-29, release date: 2017-04-12, Last modification date: 2024-10-23) |
| Primary citation | Skjoldager, N.,Blanner Bang, M.,Rykr, M.,Bjornberg, O.,Davies, M.J.,Svensson, B.,Harris, P.,Hagglund, P. The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage. Sci Rep, 7:46282-46282, 2017 Cited by PubMed Abstract: 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 C7α 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. PubMed: 28397795DOI: 10.1038/srep46282 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.81 Å) |
Structure validation
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