1KNC
Structure of AhpD from Mycobacterium tuberculosis, a novel enzyme with thioredoxin-like activity.
Summary for 1KNC
| Entry DOI | 10.2210/pdb1knc/pdb |
| Descriptor | AhpD protein, SULFATE ION (3 entities in total) |
| Functional Keywords | ahpd, thioredoxin, disulfide, peroxiredoxin, lpd, redox, electron transport |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 3 |
| Total formula weight | 58037.63 |
| Authors | Bryk, R.,Lima, C.D.,Erdjument-Bromage, H.,Tempst, P.,Nathan, C. (deposition date: 2001-12-18, release date: 2002-01-23, Last modification date: 2024-02-14) |
| Primary citation | Bryk, R.,Lima, C.D.,Erdjument-Bromage, H.,Tempst, P.,Nathan, C. Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein. Science, 295:1073-1077, 2002 Cited by PubMed Abstract: Mycobacterium 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. PubMed: 11799204DOI: 10.1126/science.1067798 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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