Cryo-EM Structures and Regulation of Arabinofuranosyltransferase AftD from Mycobacteria
Yong Zi Tan,
Ruixiang Blake Zheng,
Sabrina I. Giacometti,
Ana L. Rosário,
Venkata P Dandey,
Ashleigh M. Raczkowski,
Maria João Catalão,
Oliver B Clarke,
Todd L. Lowary,
Clinton S. Potter,
Posted 23 Dec 2019
bioRxiv DOI: 10.1101/2019.12.22.885152 (published DOI: 10.1016/j.molcel.2020.04.014)
Posted 23 Dec 2019
Mycobacterium tuberculosis causes tuberculosis, a disease that kills over one 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 conserved GT-C glycosyltransferase fold and three carbohydrate binding modules. Glycan array analysis shows that AftD binds complex arabinose glycans. Additionally, AftD is non-covalently complexed with an acyl carrier protein (ACP). 3.4 and 3.5 Å structures of a mutant with impaired ACP binding reveal a conformational change that suggests the ACP may regulate AftD function. Using a conditional knock-out constructed in M. smegmatis, mutagenesis experiments confirm the essentiality of the putative active site and the ACP binding for AftD function.
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