Crystal structure of PapA5, a phthiocerol dimycocerosyl transferase from Mycobacterium tuberculosis.

@article{Buglino2004CrystalSO,
  title={Crystal structure of PapA5, a phthiocerol dimycocerosyl transferase from Mycobacterium tuberculosis.},
  author={John A. Buglino and Kenolisa C Onwueme and Juli{\'a}n A. Ferreras and Luis E.N. Quadri and Christopher D Lima},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 29},
  pages={30634-42}
}
Polyketide-associated protein A5 (PapA5) is an acyltransferase that is involved in production of phthiocerol and phthiodiolone dimycocerosate esters, a class of virulence-enhancing lipids produced by Mycobacterium tuberculosis. Structural analysis of PapA5 at 2.75-A resolution reveals a two-domain structure that shares unexpected similarity to structures of chloramphenicol acetyltransferase, dihydrolipoyl transacetylase, carnitine acetyltransferase, and VibH, a non-ribosomal peptide synthesis… CONTINUE READING