Insights into the mechanisms of the selectivity filter of Escherichia coli aquaporin Z
作者： Guodong Hu , Liao Y. Chen , Jihua Wang
DOI: 10.1007/S00894-012-1379-2
关键词:
摘要: Aquaporin Z (AQPZ) is a tetrameric protein that forms water channels in the cell membrane of Escherichia coli. The histidine residue (residue 174) selectivity filter (SF) region plays an important role transport across membrane. In this work, we perform equilibrium molecular dynamics (MD) simulations to illustrate gating mechanism SF and influences 174 two different protonation states: Hsd174 with proton at Nδ, Hse174 Ne. We calculate pore radii versus simulation time. steered MD compute free-energy profile, i.e., potential mean force (PMF) molecule through region. conduct quantum mechanics calculation binding energy one residues hydrogen bonds formed between side chain 189 (Arg189) play roles AQPZ. pores, hydrogen-bond analysis, free energies show it easier for molecules permeate AQPZ Hse state than Hsd state.
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