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Electron and atomic force microscopy of the trimeric ammonium transporter AmtB
Author(s) -
Conroy Matthew J,
Jamieson Stuart J,
Blakey Daniel,
Kaufmann Thomas,
Engel Andreas,
Fotiadis Dimitrios,
Merrick Mike,
Bullough Per A
Publication year - 2004
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400296
Subject(s) - atomic force microscopy , transporter , ammonium , chemistry , biophysics , nanotechnology , physics , crystallography , biology , biochemistry , materials science , gene , organic chemistry
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.