AI Article Synopsis
- 4'-Phosphopantetheinyl transferases (PPTases) are enzymes that modify carrier proteins and are crucial for biological processes across all life forms.
- The study focuses on the Sfp-type PPTases from Mycobacterium tuberculosis and Mycobacterium ulcerans, revealing unique structural features that differentiate them from other known PPTases.
- These findings indicate that Mycobacterial PPTases may be promising targets for developing new treatments against infections caused by these pathogens.
Article Abstract
4'-Phosphopantetheinyl transferases (PPTase) post-translationally modify carrier proteins with a phosphopantetheine moiety, an essential reaction in all three domains of life. In the bacterial genus Mycobacteria, the Sfp-type PPTase activates pathways necessary for the biosynthesis of cell wall components and small molecule virulence factors. We solved the X-ray crystal structures and biochemically characterized the Sfp-type PPTases from two of the most prevalent Mycobacterial pathogens, PptT of M. tuberculosis and MuPPT of M. ulcerans. Structural analyses reveal significant differences in cofactor binding and active site composition when compared to previously characterized Sfp-type PPTases. Functional analyses including the efficacy of Sfp-type PPTase-specific inhibitors also suggest that the Mycobacterial Sfp-type PPTases can serve as therapeutic targets against Mycobacterial infections.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4168790 | PMC |
| http://dx.doi.org/10.1021/cb500263p | DOI Listing |
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