ArticleJournal of molecular modeling2012
Insights into the mechanisms of the selectivity filter of Escherichia coli aquaporin Z.
Article in Journal of molecular modeling, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Hydrogen peroxide transport by aquaporins: insights from molecular modeling and simulations.Biophysical reviews · 2025Review
- Water in Nanopores and Biological Channels: A Molecular Simulation Perspective.Chemical reviews · 2020Review
- Presence of Intra-helical Salt-Bridge in Loop E Half-Helix Can Influence the Transport Properties of AQP1 and GlpF Channels: Molecular Dynamics Simulations of In Silico Mutants.The Journal of membrane biology · 2019Article
- Increasing Salt Rejection of Polybenzimidazole Nanofiltration Membranes via the Addition of Immobilized and Aligned Aquaporins.Processes (Basel, Switzerland) · 2019Article
- Side chain flexibility and the pore dimensions in the GABAA receptor.Journal of computer-aided molecular design · 2016Article
- Insight into conformational change for 14-3-3σ protein by molecular dynamics simulation.International journal of molecular sciences · 2014Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Aquaporin Z (AQPZ) is a tetrameric protein that forms water channels in the cell membrane of Escherichia coli. The histidine residue (residue 174) in the selectivity filter (SF) region plays an important role in the transport of water across the membrane. In this work, we perform equilibrium molecular dynamics (MD) simulations to illustrate the gating mechanism of the SF and the influences of residue 174 in two different protonation states: Hsd174 with the proton at Nδ, and Hse174 with the proton at Nε. We calculate the pore radii in the SF region versus the simulation time. We perform steered MD to compute the free-energy profile, i.e., the potential of mean force (PMF) of a water molecule through the SF region. We conduct a quantum mechanics calculation of the binding energy of one water molecule with the residues in the SF region. The hydrogen bonds formed between the side chain of Hsd174 and the side chain of residue 189 (Arg189) play important roles in the selectivity mechanism of AQPZ. The radii of the pores, the hydrogen-bond analysis, and the free energies show that it is easier for water molecules to permeate through the SF region of AQPZ with residue 174 in the Hse state than in the Hsd state.
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