Back to Search
Start Over
Crystal structure of the essential Mycobacterium tuberculosis phosphopantetheinyl transferase PptT, solved as a fusion protein with maltose binding protein.
- Source :
-
Journal of Structural Biology . Dec2014, Vol. 188 Issue 3, p274-278. 5p. - Publication Year :
- 2014
-
Abstract
- Phosphopantetheinyl transferases (PPTases) are key enzymes in the assembly-line production of complex molecules such as fatty acids, polyketides and polypeptides, where they activate acyl or peptidyl carrier proteins, transferring a 4′-phosphopantetheinyl moiety from coenzyme A (CoA) to a reactive serine residue on the carrier protein. The human pathogen Mycobacterium tuberculosis encodes two PPTases, both essential and therefore attractive drug targets. We report the structure of the type-II PPTase PptT, obtained from crystals of a fusion protein with maltose binding protein. The structure, at 1.75 Å resolution ( R = 0.156, R free = 0.191), reveals an α/β fold broadly similar to other type-II PPTases, but with differences in peripheral structural elements. A bound CoA is clearly defined with its pantetheinyl arm tucked into a hydrophobic pocket. Interactions involving the CoA diphosphate, bound Mg 2+ and three active site acidic side chains suggest a plausible pathway for proton transfer during catalysis. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 10478477
- Volume :
- 188
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- Journal of Structural Biology
- Publication Type :
- Academic Journal
- Accession number :
- 99742394
- Full Text :
- https://doi.org/10.1016/j.jsb.2014.10.004