Download MendeleyStructure of Mycobacterium tuberculosisphosphopantetheine adenylyltransferase in complex with the feedback inhibitor CoA reveals only one active-site conformation.
Wubben, T., Mesecar, A.D.(2011) Acta Crystallogr Sect F Struct Biol Cryst Commun 67: 541-545
- PubMed: 21543857
- DOI: https://doi.org/10.1107/S1744309111010761
- Primary Citation of Related Structures:
3PNB - PubMed Abstract:
Phosphopantetheine adenylyltransferase (PPAT) catalyzes the penultimate step in the coenzyme A (CoA) biosynthetic pathway, reversibly transferring an adenylyl group from ATP to 4'-phosphopantetheine to form dephosphocoenzyme A (dPCoA). To complement recent biochemical and structural studies on Mycobacterium tuberculosis PPAT (MtPPAT) and to provide further insight into the feedback regulation of MtPPAT by CoA, the X-ray crystal structure of the MtPPAT enzyme in complex with CoA was determined to 2.11 Å resolution. Unlike previous X-ray crystal structures of PPAT-CoA complexes from other bacteria, which showed two distinct CoA conformations bound to the active site, only one conformation of CoA is observed in the MtPPAT-CoA complex.
Organizational Affiliation:
Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, Illinois, USA.
