4QVH

Crystal structure of the essential Mycobacterium tuberculosis phosphopantetheinyl transferase PptT, solved as a fusion protein with maltose binding protein

Summary for 4QVH

• Entry DOI: 10.2210/pdb4qvh/pdb
• Related PRD ID: PRD_900001
• Descriptor: Maltose-binding periplasmic protein, 4'-phosphopantetheinyl transferase chimera, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, COENZYME A, ... (7 entities in total)
• Functional Keywords: a/b-fold, phosphopantetheinyl transferase, acyl carrier protein, peptidyl carrier protein, transferase
• Biological source: Escherichia coli; More
• Total number of polymer chains: 2
• Total formula weight: 133629.64

Authors

Jung, J.,Bashiri, G.,Johnston, J.M.,Baker, E.N. (deposition date: 2014-07-15, release date: 2014-12-17, Last modification date: 2024-02-28)

Primary citation

Jung, J.,Bashiri, G.,Johnston, J.M.,Brown, A.S.,Ackerley, D.F.,Baker, E.N.
Crystal structure of the essential Mycobacterium tuberculosis phosphopantetheinyl transferase PptT, solved as a fusion protein with maltose binding protein.
J.Struct.Biol., 188:274-278, 2014

PubMed 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 1.75Å resolution (R=0.156, Rfree=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.

PubMed: 25450595
DOI: 10.1016/j.jsb.2014.10.004

Experimental method

X-RAY DIFFRACTION (1.75 Å)