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| [[Image:1knc.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1knc| PDB=1knc | SCENE= }} | | {{STRUCTURE_1knc| PDB=1knc | SCENE= }} |
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| '''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.=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11799204}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11799204 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11799204}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Redox]] | | [[Category: Redox]] |
| [[Category: Thioredoxin]] | | [[Category: Thioredoxin]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:56:40 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:35:30 2008'' |