Abstract
Escherichia coli AmtB is an archetypal member of the ammonium transporter (Amt) family, a family of proteins that are conserved in all domains of life. Reconstitution of AmtB in the presence of lipids produced large, ordered two-dimensional crystals. From these, a 12 Å resolution projection map was determined by cryoelectron microscopy, and high-resolution topographs were acquired using atomic force microscopy. Both techniques showed the trimeric structure of AmtB in which each monomer seems to have a pseudo-two-fold symmetry. This arrangement is likely to represent the in vivo structure. This work provides the first views of the structure of any member of the Amt family. © 2004 European Molecular Biology Organization.
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Conroy, M. J., Jamieson, S. J., Blakey, D., Kaufmann, T., Engel, A., Fotiadis, D., … Bullough, P. A. (2004). Electron and atomic force microscopy of the trimeric ammonium transporter AmtB. EMBO Reports, 5(12), 1153–1158. https://doi.org/10.1038/sj.embor.7400296
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