Archer Lab from the Macromolecular Crystallography Unit at ITQB NOVA collaborates with Mancia group from Columbia University and New York Structural Biology Center (USA) to unravel the structure of Arabinofuranosyltransferases, together with researchers from Simons Electron Microscopy Center (USA), iMed.ULisboa (Portugal), Alberta University (Canada) and University of Alabama at Birmingham (USA).
The 3D structure of glycosyltransferase AftD, embedded in the membrane of mycobacteria, was determined by cryogenic electron microscopy, a study coordinated by Mancia. This protein is essential for building the bacterial cell wall and it is an attractive target to design novel drugs to fight tuberculosis.
AftD has a large periplasmic domain (pink upper surface) that bind to complex glycans, eleven transmembrane helices with a conserved glycosyltransferase fold (gray) and four helices (darker orange), which are unexpectedly associated with an acyl carrier protein (orange dots).
The collaboration with Mancia group continues and it is supported by PROMETEUS, allowing students and postdocs to be trained on the emerging cryo-EM technology.
Artwork by Davide Cruz