An embedded lipid in the multidrug transporter LmrP suggests a mechanism for polyspecificity

An embedded lipid in the multidrug transporter LmrP suggests a mechanism for polyspecificity

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Bibliografiske detaljer
Main Authors:	Vincent Debruycker, Andrew Hutchin, Matthieu Masureel, Emel Ficici, Chloé Martens, Pierre Legrand, Richard A. Stein, Hassane S. Mchaourab, José D. Faraldo‐Gómez, Han Remaut, Cédric Govaerts
Format:	Artigo
Sprog:	engelsk
Udgivet:	2020
Online adgang:	https://doi.org/10.1038/s41594-020-0464-y
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Lignende værker

An embedded lipid in the multidrug transporter LmrP suggests a mechanism for polyspecificity
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Relocation of active site carboxylates in major facilitator superfamily multidrug transporter LmrP reveals plasticity in proton interactions
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Lipids modulate the conformational dynamics of a secondary multidrug transporter
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Lipids modulate the conformational dynamics of a secondary multidrug transporter
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Basic Residues R260 and K357 Affect the Conformational Dynamics of the Major Facilitator Superfamily Multidrug Transporter LmrP
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Broadly conserved Na(+)-binding site in the N-lobe of prokaryotic multidrug MATE transporters
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Lipid Composition Regulates the Orientation of Transmembrane Helices in HorA, an ABC Multidrug Transporter
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Dynamic multidrug recognition by multidrug transcriptional repressor LmrR
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Dynamic multidrug recognition by multidrug transcriptional repressor LmrR
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Bacillus subtilis LmrA Is a Repressor of the lmrAB and yxaGH Operons: Identification of Its Binding Site and Functional Analysis of lmrB and yxaGH
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Serum PLR and LMR in Behçet's disease
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Dynamic equilibrium on DNA defines transcriptional regulation of a multidrug binding transcriptional repressor, LmrR
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LmrS Is a Multidrug Efflux Pump of the Major Facilitator Superfamily from <i>Staphylococcus aureus</i>
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Allosteric regulation of G protein–coupled receptor activity by phospholipids
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The molecular basis for a polyspecific antibody.
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