6W98

Single-Particle Cryo-EM Structure of Arabinofuranosyltransferase AftD from Mycobacteria

Summary for 6W98

• Entry DOI: 10.2210/pdb6w98/pdb
• EMDB information: 21580
• Descriptor: F5/8 type C domain-containing protein, Acyl carrier protein, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: glycosyltransferase, lipomannan, lipoarabinomannan, arabinofuranose, membrane protein, nanodisc, single-particle cryo-electron microscopy, acyl carrier protein
• Biological source: Mycobacteroides abscessus subsp. abscessus; More
• Total number of polymer chains: 2
• Total formula weight: 159386.24

Authors

Tan, Y.Z.,Zhang, L.,Rodrigues, J.,Zheng, R.B.,Giacometti, S.I.,Rosario, A.L.,Kloss, B.,Dandey, V.P.,Wei, H.,Brunton, R.,Raczkowski, A.M.,Athayde, D.,Catalao, M.J.,Pimentel, M.,Clarke, O.B.,Lowary, T.L.,Archer, M.,Niederweis, M.,Potter, C.S.,Carragher, B.,Mancia, F. (deposition date: 2020-03-22, release date: 2020-05-13, Last modification date: 2025-04-02)

Primary citation

Tan, Y.Z.,Zhang, L.,Rodrigues, J.,Zheng, R.B.,Giacometti, S.I.,Rosario, A.L.,Kloss, B.,Dandey, V.P.,Wei, H.,Brunton, R.,Raczkowski, A.M.,Athayde, D.,Catalao, M.J.,Pimentel, M.,Clarke, O.B.,Lowary, T.L.,Archer, M.,Niederweis, M.,Potter, C.S.,Carragher, B.,Mancia, F.
Cryo-EM Structures and Regulation of Arabinofuranosyltransferase AftD from Mycobacteria.
Mol.Cell, 78:683-, 2020

PubMed Abstract: 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 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, suggesting that ACP may regulate AftD function. Mutagenesis experiments using a conditional knockout constructed in M. smegmatis confirm the essentiality of the putative active site and the ACP binding for AftD function.

PubMed: 32386575
DOI: 10.1016/j.molcel.2020.04.014

Experimental method

ELECTRON MICROSCOPY (2.9 Å)