3PNB

Phosphopantetheine Adenylyltransferase from Mycobacterium tuberculosis in complex with coenzyme A

Summary for 3PNB

• Entry DOI: 10.2210/pdb3pnb/pdb
• Related: 3NBA 3NBK
• Descriptor: Phosphopantetheine adenylyltransferase, COENZYME A (3 entities in total)
• Functional Keywords: transferase, adenylyltransferase
• Biological source: Mycobacterium tuberculosis
• Cellular location: Cytoplasm (By similarity): P0A530
• Total number of polymer chains: 4
• Total formula weight: 80394.58

Authors

Wubben, T.J.,Mesecar, A.D. (deposition date: 2010-11-18, release date: 2011-06-22, Last modification date: 2024-02-21)

Primary citation

Wubben, T.,Mesecar, A.D.
Structure of Mycobacterium tuberculosisphosphopantetheine adenylyltransferase in complex with the feedback inhibitor CoA reveals only one active-site conformation.
Acta Crystallogr.,Sect.F, 67:541-545, 2011

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.

PubMed: 21543857
DOI: 10.1107/S1744309111010761

Experimental method

X-RAY DIFFRACTION (2.11 Å)