amtB Antibody

1. Amt and Rh proteins are not functionally equivalent and that permeation takes place according to two distinct mechanisms. PMID: 24021113
2. the twin-histidine element serves as a filter to prevent K(+) conduction in Escherichia coli ammonium channel AmtB PMID: 23546877
3. Data explore the similarity and difference of the conduction mechanism of methylamine and ammonia molecules through AmtB, using molecular dynamics simulations. PMID: 20973592
4. 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 PMID: 15361618
5. 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 PMID: 15563598
6. 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. PMID: 16563828
7. 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. PMID: 16864585
8. simulations showed that the entrance of NH(4)(+) into the periplasmic recruitment vestibule requires only 3.1 kcal/mol of energy PMID: 16910683
9. in Escherichia coli AmtB, both histidines are absolutely required for optimum substrate conductance PMID: 17040913
10. 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 PMID: 17220269
11. 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. PMID: 17453422
12. 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. PMID: 17707821
13. AmtB allows accumulation of CH(3)NH(3)(+) ion in response to the electrical potential across the membrane PMID: 17998534
14. AmtB activity absolutely requires F215 but not F107 PMID: 18362341

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KEGG: ecj:JW0441

STRING: 316385.ECDH10B_0407