4qjk | pdb_00004qjk

Crystal structure of M. tuberculosis phosphopantetheinyl transferase PptT

spinqualitylabelsall models 4qjk, resolution 1.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4qjk is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: COA, SO4 NonStd Res: MSE Related: 4qjl Activity: [acyl-carrier-protein_synthase Holo-[acyl-carrier-protein] synthase], with EC number 2.7.8.7 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Structure, Biochemistry, and Inhibition of Essential 4'-Phosphopantetheinyl Transferases from Two Species of Mycobacteria.,Vickery CR, Kosa NM, Casavant EP, Duan S, Noel JP, Burkart MD ACS Chem Biol. 2014 Jul 9. PMID:24963544 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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