| simulations reveal previously undiscovered POPG binding sites on the intracellular side of the lipid bilayer between the AmtB subunits. | The lipid environment determines the activity of the Escherichia coli ammonium transporter AmtB.
Mirandela GD, Tamburrino G, Hoskisson PA, Zachariae U, Javelle A., Free PMC Article | 08/10/2019 |
| Amt and Rh proteins are not functionally equivalent and that permeation takes place according to two distinct mechanisms. | Different hydration patterns in the pores of AmtB and RhCG could determine their transport mechanisms.
Baday S, Wang S, Lamoureux G, Bernèche S. | 02/8/2014 |
| the twin-histidine element serves as a filter to prevent K(+) conduction in Escherichia coli ammonium channel AmtB | The molecular basis of K+ exclusion by the Escherichia coli ammonium channel AmtB.
Hall JA, Yan D., Free PMC Article | 08/10/2013 |
| Data explore the similarity and difference of the conduction mechanism of methylamine and ammonia molecules through AmtB, using molecular dynamics simulations. | Molecular dynamics simulations on the mechanism of transporting methylamine and ammonia by ammonium transporter AmtB.
Wang J, Yang H, Zuo Z, Yan X, Wang Y, Luo X, Jiang H, Chen K, Zhu W. | 03/5/2011 |
| AmtB activity absolutely requires F215 but not F107 | Substrate binding, deprotonation, and selectivity at the periplasmic entrance of the Escherichia coli ammonia channel AmtB.
Javelle A, Lupo D, Ripoche P, Fulford T, Merrick M, Winkler FK., Free PMC Article | 01/21/2010 |
| AmtB allows accumulation of CH(3)NH(3)(+) ion in response to the electrical potential across the membrane | The W148L substitution in the Escherichia coli ammonium channel AmtB increases flux and indicates that the substrate is an ion.
Fong RN, Kim KS, Yoshihara C, Inwood WB, Kustu S., Free PMC Article | 01/21/2010 |
| N-terminus verified by Edman degradation on mature peptide | See all PubMed (2) articlesThe ammonia channel protein AmtB from Escherichia coli is a polytopic membrane protein with a cleavable signal peptide.
Thornton J, Blakey D, Scanlon E, Merrick M. Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 A.
Khademi S, O'Connell J 3rd, Remis J, Robles-Colmenares Y, Miercke LJ, Stroud RM, Khademi S, O'Connell J 3rd, Remis J, Robles-Colmenares Y, Miercke LJ, Stroud RM. | 11/5/2007 |
| The GlnK protein binding causes a significant downshift in the Am6 pK(a) value of the AmtB. However, this downshift is perfectly compensated by the reorientation of the protein backbone upon AmtB-GlnK complex formation. | Modulation of the protein environment in the hydrophilic pore of the ammonia transporter protein AmtB upon GlnK protein binding.
Ishikita H. | 01/21/2010 |
| Co-purification of AmtB with GlnK from ammonium-shocked E. coli cells definitvely demonstrates that these two proteins form a functional complex with a stoichiometry of 1:1. | In vitro analysis of the Escherichia coli AmtB-GlnK complex reveals a stoichiometric interaction and sensitivity to ATP and 2-oxoglutarate.
Durand A, Merrick M. | 01/21/2010 |
| simulations showed that the entrance of NH(4)(+) into the periplasmic recruitment vestibule requires only 3.1 kcal/mol of energy | Molecular dynamics simulations on the Escherichia coli ammonia channel protein AmtB: mechanism of ammonia/ammonium transport.
Lin Y, Cao Z, Mo Y. | 01/21/2010 |
| GlnK interacts with AmtB almost exclusively via a long surface loop containing Y51 (T-loop), the tip of which inserts deeply into the cytoplasmic pore exit, blocking ammonia conduction | The crystal structure of the Escherichia coli AmtB-GlnK complex reveals how GlnK regulates the ammonia channel.
Conroy MJ, Durand A, Lupo D, Li XD, Bullough PA, Winkler FK, Merrick M., Free PMC Article | 01/21/2010 |
| the C-terminus play a significant role in normal AmtB function and the C-terminal region might also mediate co-operativity between the three subunits of AmtB. | The conserved carboxy-terminal region of the ammonia channel AmtB plays a critical role in channel function.
Severi E, Javelle A, Merrick M. | 01/21/2010 |
| structure of an ammonia channel AmtB, determined to 1.35 angstrom resolution, shows it to be a channel that spans the membrane 11 times; reconstitution of AmtB into vesicles shows that AmtB conducts uncharged NH3 | Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 A.
Khademi S, O'Connell J 3rd, Remis J, Robles-Colmenares Y, Miercke LJ, Stroud RM, Khademi S, O'Connell J 3rd, Remis J, Robles-Colmenares Y, Miercke LJ, Stroud RM. | 01/21/2010 |
| in Escherichia coli AmtB, both histidines are absolutely required for optimum substrate conductance | An unusual twin-his arrangement in the pore of ammonia channels is essential for substrate conductance.
Javelle A, Lupo D, Zheng L, Li XD, Winkler FK, Merrick M. | 01/21/2010 |
| Review. The Escherichia coli ammonium transport protein (AmtB) has become the model system of choice for analysis of the process of ammonium uptake by the ubiquitous Amt family of inner membrane proteins. | The Escherichia coli AmtB protein as a model system for understanding ammonium transport by Amt and Rh proteins.
Merrick M, Javelle A, Durand A, Severi E, Thornton J, Avent ND, Conroy MJ, Bullough PA. | 01/21/2010 |
| solved the structure of wild-type AmtB from Escherichia coli in two crystal forms at 1.8- and 2.1-A resolution; binding site and hydrophobic pore are described; adiabatic free energy calculations support an electrostatic barrier model for specificity | The mechanism of ammonia transport based on the crystal structure of AmtB of Escherichia coli.
Zheng L, Kostrewa D, Bernèche S, Winkler FK, Li XD., Free PMC Article | 01/21/2010 |