ArticleProtein science : a publication of the Protein Society2016
Molecular dynamic study of MlaC protein in Gram-negative bacteria: conformational flexibility, solvent effect and protein-phospholipid binding.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Article
- Coordinated subdomain movements of MlaC regulate ligand binding and transport.Computational and structural biotechnology journal · 2025Article
- Investigating Lipid Transporter Protein and Lipid Interactions Using Variable Temperature Electrospray Ionization, Ultraviolet Photodissociation Mass Spectrometry, and Collision Cross Section Analysis.Analytical chemistry · 2024Article
- The conformational plasticity of structurally unrelated lipid transport proteins correlates with their mode of action.PLoS biology · 2024Article
- The Mla system and its role in maintaining outer membrane barrier function inFrontiers in cellular and infection microbiology · 2024Article
- Molecular mechanism of phospholipid transport at the bacterial outer membrane interface.Nature communications · 2023Article
- The Mla system of diderm Firmicute Veillonella parvula reveals an ancestral transenvelope bridge for phospholipid trafficking.Nature communications · 2023Article
- Structure and lipid dynamics in the maintenance of lipid asymmetry inner membrane complex of A. baumannii.Communications biology · 2021Article
- Structural mechanism of phospholipids translocation by MlaFEDB complex.Cell research · 2020Article
- Article
- The Mla pathway ineLife · 2020Article
- Lipid trafficking across the Gram-negative cell envelope.The Journal of biological chemistry · 2019Review
- Intermembrane transport: Glycerophospholipid homeostasis of the Gram-negative cell envelope.Proceedings of the National Academy of Sciences of the United States of America · 2019Review
- Docking simulation and antibiotic discovery targeting the MlaC protein in Gram-negative bacteria.Chemical biology & drug design · 2019Article
- TheeLife · 2019Article
- The architecture of the OmpC-MlaA complex sheds light on the maintenance of outer membrane lipid asymmetry inThe Journal of biological chemistry · 2018Article
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Authors and funding
6 authors.
Funding
Abstract
The composition of the outer membrane in Gram-negative bacteria is asymmetric, with the lipopolysaccharides found in the outer leaflet and phospholipids in the inner leaflet. The MlaC protein transfers phospholipids from the outer to inner membrane to maintain such lipid asymmetry in the Mla pathway. In this work, we have performed molecular dynamics simulations on apo and phospholipid-bound systems to study the dynamical properties of MlaC. Our simulations show that the phospholipid forms hydrophobic interactions with the protein. Residues surrounding the entrance of the binding site exhibit correlated motions to control the site opening and closing. Lipid binding leads to increase of the binding pocket volume and precludes entry of the water molecules. However, in the absence of the phospholipid, water molecules can freely move in and out of the binding site when the pocket is open. Dehydration occurs when the pocket closes. This study provides dynamic information of the MlaC protein and may facilitate the design of antibiotics against the Mla pathway of Gram-negative bacteria.
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