skip to main content

SciTech ConnectSciTech Connect

Title: Structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase in complex with the feedback inhibitor CoA reveals only one active-site conformation

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 {angstrom} 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.
Authors:
;  [1] ;  [2]
  1. (Purdue)
  2. (
Publication Date:
OSTI Identifier:
1031937
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallogr. F; Journal Volume: 67; Journal Issue: (5) ; 05, 2011
Research Org:
Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
Sponsoring Org:
NIH
Country of Publication:
United States
Language:
ENGLISH
Subject:
60 APPLIED LIFE SCIENCES; BACTERIA; COENZYMES; CRYSTAL STRUCTURE; ENZYMES; FEEDBACK; MYCOBACTERIUM TUBERCULOSIS; REGULATIONS; RESOLUTION