Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA

Autor: David Albesa-Jové, Zuzana Svetlíková, Montse Tersa, Enea Sancho-Vaello, Ana Carreras-González, Pascal Bonnet, Pedro Arrasate, Ander Eguskiza, Shiva K. Angala, Javier O. Cifuente, Jana Korduláková, Mary Jackson, Katarína Mikušová, Marcelo E. Guerin
Jazyk: angličtina
Rok vydání: 2016
Předmět:
Zdroj: Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
Druh dokumentu: article
ISSN: 2041-1723
DOI: 10.1038/ncomms10906
Popis: PatA is a membrane-associated acyltransferase that is essential for the biosynthesis of mycobacterial glycolipids. Here, Albesa-Jovéet al. describe structures of PatA from Mycobacterium smegmatisin complex with acyl donors and show that catalysis occurs by an unusual charge-relay mechanism.
Databáze: Directory of Open Access Journals