ArticleFrontiers in bioengineering and biotechnology2016
Characteristics of Sucrose Transport through the Sucrose-Specific Porin ScrY Studied by Molecular Dynamics Simulations.
Article in Frontiers in bioengineering and biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- The structures and functions of Salmonella outer membrane.Archives of microbiology · 2026Review
- A Sucrose-Utilisation Gene Cluster Contributes to Colonisation of Horse Chestnut by Pseudomonas syringae pv. aesculi.Molecular plant pathology · 2025Article
- Harnessing the Power of Our Immune System: The Antimicrobial and Antibiofilm Properties of Nitric Oxide.Microorganisms · 2024Review
- Molecular simulation of lignin-related aromatic compound permeation through gram-negative bacterial outer membranes.The Journal of biological chemistry · 2022Article
- The C2 entity of chitosugars is crucial in molecular selectivity of the Vibrio campbellii chitoporin.The Journal of biological chemistry · 2021Article
- The Whole Is Bigger than the Sum of Its Parts: Drug Transport in the Context of Two Membranes with Active Efflux.Chemical reviews · 2021Article
- Is the E. coli Homolog of the Formate/Nitrite Transporter Family an Anion Channel? A Computational Study.Biophysical journal · 2020Article
- Phosphatidylinositol-3,5-bisphosphate lipid-binding-induced activation of the human two-pore channel 2.Cellular and molecular life sciences : CMLS · 2018Article
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Sucrose-specific porin (ScrY) is a transmembrane protein that allows for the uptake of sucrose under growth-limiting conditions. The crystal structure of ScrY was resolved before by X-ray crystallography, both in its uncomplexed form and with bound sucrose. However, little is known about the molecular characteristics of the transport mechanism of ScrY. To date, there has not yet been any clear demonstration for sucrose transport through the ScrY. Here, the dynamics of the ScrY trimer embedded in a phospholipid bilayer as well as the characteristics of sucrose translocation were investigated by means of atomistic molecular dynamics (MD) simulations. The potential of mean force (PMF) for sucrose translocation through the pore showed two main energy barriers within the constriction region of ScrY. Energy decomposition allowed to pinpoint three aspartic acids as key residues opposing the passage of sucrose, all located within the L3 loop. Mutation of two aspartic acids to uncharged residues resulted in an accordingly modified electrostatics and decreased PMF barrier. The chosen methodology and results will aid in the design of porins with modified transport specificities.
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