Cryo-EM Structures and Regulation of Arabinofuranosyltransferase AftD from Mycobacteria

Yong Zi Tan, Lei Zhang, José António Vieira Rodrigues, Ruixiang Blake Zheng, Sabrina I. Giacometti, Ana L. Rosário, Brian Kloss, Venkata P. Dandey, Hui Wei, Richard Brunton, Ashleigh M. Raczkowski, Diogo Athayde, Maria João Catalão, Madalena Pimentel, Oliver B. Clarke, Todd L. Lowary, Margarida Archer, Michael Niederweis, Clinton S. Potter, Bridget CarragherFilippo Mancia

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)


Tan et al. present the cryo-EM structures of essential wild-type and mutant mycobacterial arabinofuranosyltransferase D (AftD), revealing the putative active site geometry and carbohydrate-binding modules. Acyl carrier protein (ACP) was tightly associated with AftD. Impairing ACP binding blocks AftD's active site, suggesting that ACP regulates enzyme function.

Original languageEnglish
Pages (from-to)683-699.e11
JournalMolecular Cell
Issue number4
Publication statusPublished - 21 May 2020


  • acyl carrier protein
  • arabinofuranose
  • glycosyltransferase
  • lipoarabinomannan
  • lipomannan
  • membrane protein
  • Mycobacterium tuberculosis
  • nanodisc
  • single-particle cryo-electron microscopy


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