• AmtB

    SURFE²R N1 recordings of the ammonium transporter AmtB. AmtB was purified from E.Coli and incororated into liposomes. Data from Mirandela et al, 2018.

AmtB - Ammonia/Ammonium Transporter

Family:
Ammonia transporters

Members:
Amt (ammonia transporters) in bacteria and plants, MEPs (methylammonium/ammonium permeases) in yeast and Rh (Rhesus proteins) in chordates.

Topology:
Protein exists as a trimer, each subunit contains 11 transmembrane (TM) segments and containining a pseudo two-fold symmetry. Each monomer contains a hydrophobic ammonia conducting pore.

Data and Applications

AmtB - Substrate specificity

AmtB specificity for ammonium

Icon N1 SURFE2R N1 data and applications:

Purified AmtB from E.Coli was incorporated into liposomes and used on the SURFE2R N1. AmtB substrate specificity. (A) Transient current measured after a 100 mM substrate jump. Ammonium (red), methylammonium (black), potassium (green) or sodium (purple). Potassium and sodium do not act as substrates for AmtB and methylammonium translocates but at a much reduced rate compared with ammonium. Insert: Normalised current after a 100 mM substrate jump. Ammonium (red), methylammonium (black).

Data from Mirandela et al, 2018

AmtB - Activation by ammonium

AmtB activation by ammonium

Icon N1 SURFE2R N1 data and applications:

Purified AmtB from E.Coli was incorporated into liposomes and used on the SURFE2R N1. Shown are transient currents measured after a 100 mM ammonium jump in empty liposomes (green) or proteoliposomes containing AmtB at a lipid protein ratio (LPR) of 50 (black), 10 (red) or 5 (blue). Insert: Normalized current measured in proteoliposomes containing AmtB at an LPR of 50 (black), 10 (red) or 5 (blue).

Data from Mirandela et al, 2018

Testimonials

Dr. Arnaud Javelle - Statement about the SURFE²R N1 Device

Icon N1  “Using the SURFE2R N1 we have recently obtained high quality data in a very short period of time. We have developed an assay to measure the activity of ammonium transporters from the Amt protein family. There has been considerable controversy over the mechanism of ammonium transport by Amt proteins and the controversy was due to the lack of quantitative kinetic data characterizing the activity of the proteins at the single channel level. The SSM technologies allows to overcome this hurdle and we are now capable of answering very challenging functional questions concerning the mechanisms and the energetics of these transporters."

Dr. Arnaud Javelle, Chancellor's fellow, Strathclyde Institute of Pharmacy and Biomedical Sciences

Publications

2018 - The lipid environment determines the activity of the E. coli ammonium transporter, AmtB

Icon N1   SURFE²R N1 publication in Faseb J (2018)

Authors:
Mirandela G.D., Tamburrino G., Hoskisson P.A., Zachariae U., Javelle A.

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