Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.molcel.2020.04.014
Title: Cryo-EM Structures and Regulation of Arabinofuranosyltransferase AftD from Mycobacteria
Authors: Tan, Yong Zi 
Zhang, Lei
Rodrigues, Jose
Zheng, Ruixiang Blake
Giacometti, Sabrina
Rosario, Ana L
Kloss, Brian
Dandey, Venkata P
Wei, Hui
Brunton, Richard
Raczkowski, Ashleigh M
Athayde, Diogo
Catalao, Maria Joao
Pimentel, Madalena
Clarke, Oliver B
Lowary, Todd L
Archer, Margarida
Niederweis, Michael
Potter, Clinton S
Carragher, Bridget
Mancia, Filippo
Keywords: Science & Technology
Life Sciences & Biomedicine
Biochemistry & Molecular Biology
Cell Biology
ACYL CARRIER PROTEIN
WALL ARABINAN BIOSYNTHESIS
TUBERCULOSIS CELL-WALL
PHOSPHATIDYLINOSITOL MANNOSIDE
N-GLYCOSYLATION
MOLECULAR-BASIS
IDENTIFICATION
ARABINOGALACTAN
MEMBRANE
MODEL
Issue Date: 21-May-2020
Publisher: CELL PRESS
Citation: Tan, Yong Zi, Zhang, Lei, Rodrigues, Jose, Zheng, Ruixiang Blake, Giacometti, Sabrina, Rosario, Ana L, Kloss, Brian, Dandey, Venkata P, Wei, Hui, Brunton, Richard, Raczkowski, Ashleigh M, Athayde, Diogo, Catalao, Maria Joao, Pimentel, Madalena, Clarke, Oliver B, Lowary, Todd L, Archer, Margarida, Niederweis, Michael, Potter, Clinton S, Carragher, Bridget, Mancia, Filippo (2020-05-21). Cryo-EM Structures and Regulation of Arabinofuranosyltransferase AftD from Mycobacteria. MOLECULAR CELL 78 (4) : 683-+. ScholarBank@NUS Repository. https://doi.org/10.1016/j.molcel.2020.04.014
Abstract: 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.
Source Title: MOLECULAR CELL
URI: https://scholarbank.nus.edu.sg/handle/10635/227202
ISSN: 10972765
10974164
DOI: 10.1016/j.molcel.2020.04.014
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