Single-Particle Cryo-EM of Arabinofuranosyltransferase AftD from Mycobacteria, Mutant R1389S
Ontology highlight
ABSTRACT:
SUBMITTER: Yong Zi Tan
PROVIDER: EMPIAR-10391 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Cryo-EM Structures and Regulation of Arabinofuranosyltransferase AftD from Mycobacteria.
Tan Yong Zi YZ Zhang Lei L Rodrigues José J Zheng Ruixiang Blake RB Giacometti Sabrina I SI Rosário Ana L AL Kloss Brian B Dandey Venkata P VP Wei Hui H Brunton Richard R Raczkowski Ashleigh M AM Athayde Diogo D Catalão Maria João MJ Pimentel Madalena M Clarke Oliver B OB Lowary Todd L TL Archer Margarida M Niederweis Michael M Potter Clinton S CS Carragher Bridget B Mancia Filippo F
Molecular cell 20200507 4
Mycobacterium tuberculosis causes tuberculosis, a disease that kills over 1 million people each year. Its cell envelope is a common antibiotic target and has a unique structure due, in part, to two lipidated polysaccharides-arabinogalactan and lipoarabinomannan. Arabinofuranosyltransferase D (AftD) is an essential enzyme involved in assembling these glycolipids. We present the 2.9-Å resolution structure of M. abscessus AftD, determined by single-particle cryo-electron microscopy. AftD has a cons ...[more]
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