CryoEM structure of the antibacterial target PBP1b at 3.3 Å resolution

Nathanael A. Caveney; Sean D. Workman; Rui Yan; Claire E. Atkinson; Zhiheng Yu; Natalie C. J. Strynadka

doi:10.1038/s41467-021-23063-6

Nature Communications (May 2021)

CryoEM structure of the antibacterial target PBP1b at 3.3 Å resolution

Nathanael A. Caveney,
Sean D. Workman,
Rui Yan,
Claire E. Atkinson,
Zhiheng Yu,
Natalie C. J. Strynadka

Affiliations

Nathanael A. Caveney: Department of Biochemistry and Molecular Biology, University of British Columbia
Sean D. Workman: Department of Biochemistry and Molecular Biology, University of British Columbia
Rui Yan: CryoEM Shared Resources, Howard Hughes Medical Institute
Claire E. Atkinson: Department of Biochemistry and Molecular Biology, University of British Columbia
Zhiheng Yu: CryoEM Shared Resources, Howard Hughes Medical Institute
Natalie C. J. Strynadka: Department of Biochemistry and Molecular Biology, University of British Columbia

DOI: https://doi.org/10.1038/s41467-021-23063-6
Journal volume & issue: Vol. 12, no. 1
pp. 1 – 7

Abstract

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Our structural understanding of class A penicillin binding proteins is incomplete due to the difficulty in their crystallization and the complexity of their substrates. Here, authors determine the structure of the 83 kDa class A PBP from Escherichia coli, PBP1b, using cryogenic electron microscopy and a styrene maleic acid anhydride membrane mimetic.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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