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Ugur Akgun and Shahram KhademiUgur Akgun and Shahram Khademi DEPARTMENT OF BIOCHEMISTRY, THE UNIVERSITY OF IOWADEPARTMENT OF BIOCHEMISTRY, THE UNIVERSITY OF IOWA
 

Summary: Ugur Akgun and Shahram KhademiUgur Akgun and Shahram Khademi
DEPARTMENT OF BIOCHEMISTRY, THE UNIVERSITY OF IOWADEPARTMENT OF BIOCHEMISTRY, THE UNIVERSITY OF IOWA
MECHANISM OF SUBSTRATE SELECTIVITY AND RECRUITMENT
IN AMMONIA CHANNELIN AMMONIA CHANNEL
Abstract
The transport of ammonia, which is fundamental to nitrogen metabolism in all
domains of life, is provided by the Rh/Amt/MEP membrane protein superfamily.
The first structure from this protein family, AmtB from Escherichia coli, has
been determined at 1.35 Angstrom resolution using x-ray crystallography.
Here, we report total of 100 ns Molecular Dynamics simulations of trimeric
E. Coli AmtB embedded into POPE bilayer for NH3 and NH4+ conduction.
Moreover since the Rh proteins are speculated to conduct CO2, we also
simulated the conduction of CO2 through AmtB, which is a prokaryotic member of
Rh/Amt/MEP superfamily.
The results show that the selectivity of ligand uptake in Rh/Amt/MEP
membrane protein superfamily is mainly regulated by the periplasmic vestibule.
The energy profiles of NH4+, NH3, and CO2 conductions are derived by using
Steered Molecular Dynamics simulations.
IntroductionIntroduction
The transport of ammonium is a fundamental process across the biological

  

Source: Akgun, Ugur - Department of Physics and Astronomy, University of Iowa

 

Collections: Physics