3X1J

Crystal Structure of Phosphopantetheine adenylyltransferase (PPAT/CoaD) with AcCoA from Pseudomonas aeruginosa

Summary for 3X1J

Entry DOI	10.2210/pdb3x1j/pdb
Related	3X1K 3X1M 4RUK
Descriptor	Phosphopantetheine adenylyltransferase, ACETYL COENZYME *A, PHOSPHATE ION, ... (7 entities in total)
Functional Keywords	rossmann fold, transferase
Biological source	Pseudomonas aeruginosa 2192
Total number of polymer chains	3
Total formula weight	56920.45
Authors	Chatterjee, R.,Datta, S. (deposition date: 2014-11-19, release date: 2015-11-25, Last modification date: 2024-03-20)
Primary citation	Chatterjee, R.,Mondal, A.,Basu, A.,Datta, S. Transition of phosphopantetheine adenylyltransferase from catalytic to allosteric state is characterized by ternary complex formation in Pseudomonas aeruginosa Biochim.Biophys.Acta, 1864:773-786, 2016 Cited by PubMed Abstract: Phosphopantetheine adenylyltransferase (PPAT) is a rate limiting enzyme which catalyzes the conversion of ATP and pantetheine to dephosphocoenzyme and pyrophosphate. The enzyme is allosteric in nature and regulated by Coenzyme A (CoA) through feedback inhibition. So far, several structures have been solved to decipher the catalytic mechanism of this enzyme. PubMed: 27041211 DOI: 10.1016/j.bbapap.2016.03.018 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.334 Å)

Structure validation