6W98

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

6W98 の概要

• エントリーDOI: 10.2210/pdb6w98/pdb
• EMDBエントリー: 21580
• 分子名称: F5/8 type C domain-containing protein, Acyl carrier protein, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: glycosyltransferase, lipomannan, lipoarabinomannan, arabinofuranose, membrane protein, nanodisc, single-particle cryo-electron microscopy, acyl carrier protein
• 由来する生物種: Mycobacteroides abscessus subsp. abscessus; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 159386.24

構造登録者

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. (登録日: 2020-03-22, 公開日: 2020-05-13, 最終更新日: 2025-04-02)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (2.9 Å)