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

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

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.

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Bibliographic Details
Main Authors: 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
Format: article
Language:EN
Published: Nature Portfolio 2016
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Science
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Online Access:https://doaj.org/article/345eecca519f4563aed75b57f445943c
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Summary: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.

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