3X1M

Crystal structure of Phosphopantetheine adenylyltransferase/PPAT from Pseudomonas aeruginosa with CoA

Summary for 3X1M

Entry DOI	10.2210/pdb3x1m/pdb
Related	3x1J 3X1K 4RUK
Descriptor	Phosphopantetheine adenylyltransferase, COENZYME A, DIMETHYL SULFOXIDE, ... (7 entities in total)
Functional Keywords	rossmann fold transferase, transferase
Biological source	Pseudomonas aeruginosa 2192
Total number of polymer chains	3
Total formula weight	56895.56
Authors	Chatterjee, R.,Datta, S. (deposition date: 2014-11-24, release date: 2015-11-25, Last modification date: 2023-11-08)
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 (2.5 Å)

Structure validation