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6X0O

Single-Particle Cryo-EM Structure of Arabinosyltransferase EmbB from Mycobacterium smegmatis

Summary for 6X0O
Entry DOI10.2210/pdb6x0o/pdb
EMDB information21983
DescriptorIntegral membrane indolylacetylinositol arabinosyltransferase EmbB, CALCIUM ION, 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE (3 entities in total)
Functional Keywordsglycosyltransferase, membrane protein, nanodisc
Biological sourceMycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Total number of polymer chains1
Total formula weight120361.47
Authors
Primary citationTan, Y.Z.,Rodrigues, J.,Keener, J.E.,Zheng, R.B.,Brunton, R.,Kloss, B.,Giacometti, S.I.,Rosario, A.L.,Zhang, L.,Niederweis, M.,Clarke, O.B.,Lowary, T.L.,Marty, M.T.,Archer, M.,Potter, C.S.,Carragher, B.,Mancia, F.
Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis.
Nat Commun, 11:3396-3396, 2020
Cited by
PubMed Abstract: 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.
PubMed: 32636380
DOI: 10.1038/s41467-020-17202-8
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

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