Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis

Yong Zi Tan; José António Vieira Rodrigues; James E. Keener; Ruixiang Blake Zheng; Richard Brunton; Brian Kloss; Sabrina I. Giacometti; Ana L. Rosário; Lei Zhang; Michael Niederweis; Oliver B. Clarke; Todd L. Lowary; Michael T. Marty; Margarida Archer; Clinton S. Potter; Bridget Carragher; Filippo Mancia

doi:10.1038/s41467-020-17202-8

Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis

Yong Zi Tan, José António Vieira Rodrigues, James E. Keener, Ruixiang Blake Zheng, Richard Brunton, Brian Kloss, Sabrina I. Giacometti, Ana L. Rosário, Lei Zhang, Michael Niederweis, Oliver B. Clarke, Todd L. Lowary, Michael T. Marty, Margarida Archer, Clinton S. Potter, Bridget Carragher, Filippo Mancia

Instituto de Tecnologia Química e Biológica António Xavier (ITQB)

Research output: Contribution to journal › Article › peer-review

19 Citations (Scopus)

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.

Original language	English
Article number	3396
Journal	Nature Communications
Volume	11
Issue number	1
DOIs	https://doi.org/10.1038/s41467-020-17202-8
Publication status	Published - 1 Dec 2020

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10.1038/s41467-020-17202-8Licence: CC BY

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Tan, Y. Z., Rodrigues, J. A. V., Keener, J. E., Zheng, R. B., Brunton, R., Kloss, B., Giacometti, S. I., Rosário, A. L., Zhang, L., Niederweis, M., Clarke, O. B., Lowary, T. L., Marty, M. T., Archer, M., Potter, C. S., Carragher, B., & Mancia, F. (2020). Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis. Nature Communications, 11(1), Article 3396. https://doi.org/10.1038/s41467-020-17202-8

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title = "Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis",

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 {\AA} 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.",

author = "Tan, \{Yong Zi\} and Rodrigues, \{Jos{\'e} Ant{\'o}nio Vieira\} and Keener, \{James E.\} and Zheng, \{Ruixiang Blake\} and Richard Brunton and Brian Kloss and Giacometti, \{Sabrina I.\} and Ros{\'a}rio, \{Ana L.\} and Lei Zhang and Michael Niederweis and Clarke, \{Oliver B.\} and Lowary, \{Todd L.\} and Marty, \{Michael T.\} and Margarida Archer and Potter, \{Clinton S.\} and Bridget Carragher and Filippo Mancia",

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Tan, YZ, Rodrigues, JAV, Keener, JE, Zheng, RB, Brunton, R, Kloss, B, Giacometti, SI, Rosário, AL, Zhang, L, Niederweis, M, Clarke, OB, Lowary, TL, Marty, MT, Archer, M, Potter, CS, Carragher, B & Mancia, F 2020, 'Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis', Nature Communications, vol. 11, no. 1, 3396. https://doi.org/10.1038/s41467-020-17202-8

TY - JOUR

T1 - Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis

AU - Tan, Yong Zi

AU - Rodrigues, José António Vieira

AU - Keener, James E.

AU - Zheng, Ruixiang Blake

AU - Brunton, Richard

AU - Kloss, Brian

AU - Giacometti, Sabrina I.

AU - Rosário, Ana L.

AU - Zhang, Lei

AU - Niederweis, Michael

AU - Clarke, Oliver B.

AU - Lowary, Todd L.

AU - Marty, Michael T.

AU - Archer, Margarida

AU - Potter, Clinton S.

AU - Carragher, Bridget

AU - Mancia, Filippo

PY - 2020/12/1

Y1 - 2020/12/1

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/85087727627

U2 - 10.1038/s41467-020-17202-8

DO - 10.1038/s41467-020-17202-8

M3 - Article

C2 - 32636380

AN - SCOPUS:85087727627

SN - 2041-1723

VL - 11

JO - Nature Communications

JF - Nature Communications

IS - 1

M1 - 3396

ER -

Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis

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