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Single-Particle Cryo-EM of Arabinosyltransferase EmbB from Mycobacterium smegmatis, Collected using both Falcon III and K2 Detectors

ABSTRACT:

SUBMITTER: Yong Zi Tan

PROVIDER: EMPIAR-10420 | biostudies-other |

REPOSITORIES: biostudies-other

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Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis.

Tan Yong Zi YZ Rodrigues José J Keener James E JE Zheng Ruixiang Blake RB Brunton Richard R Kloss Brian B Giacometti Sabrina I SI Rosário Ana L AL Zhang Lei L Niederweis Michael M Clarke Oliver B OB Lowary Todd L TL Marty Michael T MT Archer Margarida M Potter Clinton S CS Carragher Bridget B Mancia Filippo F

Nature communications 20200707 1

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 ...[more]

PMID: 32636380

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