Conformational changes in a bacterial multidrug transporter are phosphatidylethanolamine-dependent
@article{Gbaguidi2007ConformationalCI, title={Conformational changes in a bacterial multidrug transporter are phosphatidylethanolamine-dependent}, author={B{\'e}n{\'e}dicte Gbaguidi and Pierre Hakizimana and Guy Vandenbussche and Jean Marie Ruysschaert}, journal={Cellular and Molecular Life Sciences}, year={2007}, volume={64}, pages={1571-1582} }
Abstract.LmrP is an electrogenic H+/drug antiporter that extrudes a broad spectrum of antibiotics. Five carboxylic residues are implicated in drug binding (Asp142 and Glu327) and proton motive force-mediated restructuring (Asp68, Asp128 and Asp235). ATR-FTIR (Attenuated Total Reflection — Fourier Transform Infrared) and tryptophan quenching experiments revealed that phosphatidylethanolamine (PE) is required to generate the structural intermediates induced by ionization of carboxylic residues…
38 Citations
Interactions between Phosphatidylethanolamine Headgroup and LmrP, a Multidrug Transporter
- BiologyJournal of Biological Chemistry
- 2008
It is shown that a single point mutation in LmrP, D68C, is sufficient to recapitulate precisely every biochemical and biophysical effect observed when PE is replaced by PC, including energy transfer between the protein tryptophan residues and the lipid headgroups.
Protonation drives the conformational switch in the multidrug transporter LmrP.
- Biology, ChemistryNature chemical biology
- 2014
The conformational equilibrium of LmrP, a multidrug transporter from Lactococcus lactis, is uncovered and it is found that the transporter switches between outward-open and outward-closed conformations, depending on the protonation states of specific acidic residues forming a transmembrane protonations relay.
Biochemical and biophysical studies of the prokaryotic proton dependent oligopeptide transporters
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- 2013
Bacterial POTs are established as model systems for studying the mammalian oligopeptide transporters, and a mechanistic model for peptide transport is proposed.
Hoechst 33342 Is a Hidden “Janus” amongst Substrates for the Multidrug Efflux Pump LmrP
- BiologyPloS one
- 2015
Surprisingly, and in contrast to other multidrug transporters, LmrP was found to actively accumulate, rather than extrude, Hoechst 33342 in lactococcal cells, and a hidden “Janus” amongst LMRP substrates is discovered that is translocated in reverse direction across the membrane.
Crystal structure of a prokaryotic homologue of the mammalian oligopeptide–proton symporters, PepT1 and PepT2
- Biology, ChemistryThe EMBO journal
- 2011
The crystal structure of PepTSo is presented, a functionally similar prokaryotic homologue of the mammalian peptide transporters from Shewanella oneidensis, which reveals a ligand‐bound occluded state for the MFS and provides new insights into a general transport mechanism.
Lactose permease lipid selectivity using Förster resonance energy transfer.
- Biology, ChemistryBiochimica et biophysica acta
- 2010
Molecular organization of nalidixate conjugated calixarenes in bacterial model membranes probed by molecular dynamics simulation and Langmuir monolayer studies.
- ChemistryThe journal of physical chemistry. B
- 2015
Although both calixarene derivatives increase the chain tilt and conformational disordering of the DMPE molecules, these effects are more important in the case of the monosubstituted derivative.
Plasticity of lipid-protein interactions in the function and topogenesis of the membrane protein lactose permease from Escherichia coli
- Biology, ChemistryProceedings of the National Academy of Sciences
- 2010
Lactose permease of Escherichia coli exhibits uphill transport and native conformation of P7 when expressed in a mutant of E. coli in which PC completely replaces PE even though the structure is not completely native.
Structure of the YajR transporter suggests a transport mechanism based on the conserved motif A
- BiologyProceedings of the National Academy of Sciences
- 2013
The crystal structure of Escherichia coli YajR is reported, unique in illustrating the functional role of “sequence motif A” and suggests a general mechanism for the conformational change between the inward and outward states of the MFS transporters.
Phosphatidylethanolamine Deficiency Impairs Escherichia coli Adhesion by Downregulating Lipopolysaccharide Synthesis, Which is Reversible by High Galactose/Lactose Cultivation
- BiologyCell communication & adhesion
- 2017
It is found that PE deficiency could impair E. coli adhesion on macrophages or glass coverslips by downregulating lipopolysaccharide (LPS) biosynthesis, which could be reversible by high galactose/lactose but not glucose cultivation, suggesting that targeting PE biosynthesis is also a potential antibacterial strategy.
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