Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis.
Yong Zi TanJosé RodriguesJames E KeenerRuixiang Blake ZhengRichard BruntonBrian KlossSabrina I GiacomettiAna L RosárioLei ZhangMichael NiederweisOliver Biggs ClarkeTodd L LowaryMichael Thomas MartyMargarida ArcherClinton S PotterBridget CarragherFilippo ManciaPublished in: Nature communications (2020)
Arabinosyltransferase B (EmbB) belongs to a family of membrane-bound glycosyltransferases that build the lipidated polysaccharides of the mycobacterial cell envelope, and are targets of anti-tuberculosis drug ethambutol. We present the 3.3 Å resolution single-particle cryo-electron microscopy structure of Mycobacterium smegmatis EmbB, providing insights on substrate binding and reaction mechanism. Mutations that confer ethambutol resistance map mostly around the putative active site, suggesting this to be the location of drug binding.
Keyphrases
- electron microscopy
- mycobacterium tuberculosis
- pulmonary tuberculosis
- adverse drug
- single cell
- dna binding
- cell therapy
- binding protein
- high resolution
- drug induced
- emergency department
- mesenchymal stem cells
- mass spectrometry
- hiv aids
- human immunodeficiency virus
- water soluble
- structural basis
- antiretroviral therapy