1knc
Structure of AhpD from Mycobacterium tuberculosis, a novel enzyme with thioredoxin-like activity.Structure of AhpD from Mycobacterium tuberculosis, a novel enzyme with thioredoxin-like activity.
Structural highlights
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 PubMedMycobacterium tuberculosis (Mtb) mounts a stubborn defense against oxidative and nitrosative components of the immune response. Dihydrolipoamide dehydrogenase (Lpd) and dihydrolipoamide succinyltransferase (SucB) are components of alpha-ketoacid dehydrogenase complexes that are central to intermediary metabolism. We find that Lpd and SucB support Mtb's antioxidant defense. The peroxiredoxin alkyl hydroperoxide reductase (AhpC) is linked to Lpd and SucB by an adaptor protein, AhpD. The 2.0 angstrom AhpD crystal structure reveals a thioredoxin-like active site that is responsive to lipoamide. We propose that Lpd, SucB (the only lipoyl protein detected in Mtb), AhpD, and AhpC together constitute a nicotinamide adenine dinucleotide (reduced)-dependent peroxidase and peroxynitrite reductase. AhpD thus represents a class of thioredoxin-like molecules that enables an antioxidant defense. Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein.,Bryk R, Lima CD, Erdjument-Bromage H, Tempst P, Nathan C Science. 2002 Feb 8;295(5557):1073-7. Epub 2002 Jan 17. PMID:11799204[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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