## Abstract Urease plays a central role in the pathogenesis of __Helicobacter pylori__ in humans. Maturation of this nickel metalloenzyme in bacteria requires the participation of the accessory proteins UreD (termed UreH in __H. pylori__), UreF, and UreG, which form sequential complexes with the ur
Crystal structure of HP0721, a novel secreted protein from Helicobacter pylori
โ Scribed by Gianluca Cioci; Laurent Terradot; Cyril Dian; Christoph Mueller-Dieckmann; Gordon Leonard
- Publisher
- John Wiley and Sons
- Year
- 2011
- Tongue
- English
- Weight
- 256 KB
- Volume
- 79
- Category
- Article
- ISSN
- 0887-3585
No coin nor oath required. For personal study only.
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The AhpC protein from H. pylori, a thioredoxin (Trx)-dependent alkyl hydroperoxide-reductase, is a member of the ubiquitous 2-Cys peroxiredoxins family (2-Cys Prxs), a group of thiol-specific antioxidant enzymes. Prxs exert the protective antioxidant role in cells through their peroxidase activity,
## Abstract Thymidylate synthase X (ThyX) catalyzes the methylation of dUMP to form dTMP in bacterial life cycle and is regarded as a promising target for antibiotics discovery. __Helicobacter pylori__ is a human pathogen associated with a number of human diseases. Here, we cloned and purified the