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Structure paper

TitleCryo-EM Structures and Regulation of Arabinofuranosyltransferase AftD from Mycobacteria.
Journal, issue, pagesMol Cell, Vol. 78, Issue 4, Page 683-699.e11, Year 2020
Publish dateMay 21, 2020
AuthorsYong Zi Tan / Lei Zhang / José Rodrigues / Ruixiang Blake Zheng / Sabrina I Giacometti / Ana L Rosário / Brian Kloss / Venkata P Dandey / Hui Wei / Richard Brunton / Ashleigh M Raczkowski / Diogo Athayde / Maria João Catalão / Madalena Pimentel / Oliver B Clarke / Todd L Lowary / Margarida Archer / Michael Niederweis / Clinton S Potter / Bridget Carragher / Filippo Mancia /
PubMed AbstractMycobacterium 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 ...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.
External linksMol Cell / PubMed:32386575 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3.5 Å
Structure data

21580

6w98

EMDB-21580, PDB-6w98:
Single-Particle Cryo-EM Structure of Arabinofuranosyltransferase AftD from Mycobacteria
Method: EM (single particle) / Resolution: 2.9 Å

21600

6wbx

EMDB-21600, PDB-6wbx:
Single-Particle Cryo-EM Structure of Arabinofuranosyltransferase AftD from Mycobacteria, Mutant R1389S Class 1
Method: EM (single particle) / Resolution: 3.5 Å

21601

6wby

EMDB-21601, PDB-6wby:
Single-Particle Cryo-EM Structure of Arabinofuranosyltransferase AftD from Mycobacteria, Mutant R1389S Class 2
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-6OU:
[(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate / phospholipid*YM

ChemComp-PNS:
4'-PHOSPHOPANTETHEINE / Phosphopantetheine

ChemComp-HOH:
WATER / Water

Source
  • escherichia coli (strain k12) (bacteria)
  • mycobacteroides abscessus subsp. abscessus (bacteria)
  • mycobacteroides abscessus (bacteria)
KeywordsMEMBRANE PROTEIN / Glycosyltransferase / lipomannan / lipoarabinomannan / arabinofuranose / nanodisc / single-particle cryo-electron microscopy / acyl carrier protein

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