Open AccessStructure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase in complex with the feedback inhibitor CoA reveals only one active‐site conformation
Author(s) -
Wubben T.,
Mesecar A. D.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111010761
Subject(s) - coenzyme a , active site , stereochemistry , mycobacterium tuberculosis , transferase , chemistry , crystal structure , biochemistry , enzyme , crystallography , tuberculosis , medicine , pathology , reductase
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 ( Mt PPAT) and to provide further insight into the feedback regulation of Mt PPAT by CoA, the X‐ray crystal structure of the Mt PPAT 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 Mt PPAT–CoA complex.