Protonation drives the conformational switch in the multidrug transporter LmrP.
about
Energy coupling mechanisms of MFS transportersHoechst 33342 Is a Hidden "Janus" amongst Substrates for the Multidrug Efflux Pump LmrPTMalphaDB and TMbetaDB: web servers to study the structural role of sequence motifs in α-helix and β-barrel domains of membrane proteins.Identifying and quantitating conformational exchange in membrane proteins using site-directed spin labeling.Navigating Membrane Protein Structure, Dynamics, and Energy Landscapes Using Spin Labeling and EPR Spectroscopy.A Straightforward Approach to the Analysis of Double Electron-Electron Resonance DataConformational dynamics of the nucleotide binding domains and the power stroke of a heterodimeric ABC transporter.Conformational cycle and ion-coupling mechanism of the Na+/hydantoin transporter Mhp1.Functionally important carboxyls in a bacterial homologue of the vesicular monoamine transporter (VMAT).Structure and pH-induced structural rearrangements of the putative multidrug efflux pump EmrD in liposomes probed by site-directed spin labeling.Emulating proton-induced conformational changes in the vesicular monoamine transporter VMAT2 by mutagenesis.EPR characterization of Mn(ii) complexes for distance determination with pulsed dipolar spectroscopy.Lipids modulate the conformational dynamics of a secondary multidrug transporter.A Numbering System for MFS Transporter Proteins.Singular Value Decomposition Method to Determine Distance Distributions in Pulsed Dipolar Electron Spin Resonance.Mechanism of Substrate Translocation in an Alternating Access Transporter.A New Wavelet Denoising Method for Experimental Time-Domain Signals: Pulsed Dipolar Electron Spin Resonance.Direct protein-lipid interactions shape the conformational landscape of secondary transporters
P2860
Q28080486-23B6131D-9EE7-4246-8D20-068D9D547005Q28550708-FEC69BE3-B4DB-41C4-B60B-55040415621EQ30152874-7BFAE701-D07B-45A5-9B5C-690A3A964677Q30371289-5C86BE5E-9CB0-4B5F-A4DD-924147B52A34Q30380407-F11DD8AE-BAEB-4AE2-A88C-3AC782931EDAQ31007626-D496B6D5-54D3-43F7-B372-D4925071B2CFQ33715209-710BA0C8-4A26-4FB0-892E-D2B3D23ABEF2Q34384175-DB9C10F1-3E3A-4DB6-AD26-709D174F16A3Q34634284-FA89C5E7-4A3D-454F-B97D-A8DE236474D0Q37374599-159735D0-F6A6-4BAA-8D3E-E034BB656153Q37451183-FD20BE1C-70E8-49A5-9C25-E39C310B6A18Q39316203-85F71793-71AF-408C-87AA-1753C1179300Q39614959-0F21A095-E36B-42EA-97C7-A7C92D1805A4Q42745531-858241F3-88E3-4F6F-8C7D-0332D99F7D22Q47384414-8E5640FF-83D4-496C-AA54-AFA27ED047C8Q47915794-86746597-95E0-4FE7-BD5E-1540325891F5Q48167027-CFEC6FC9-525C-49ED-B1F2-1AFDA805267AQ57295402-691F4281-6BD5-47D5-B354-52614F4A9E7F
P2860
Protonation drives the conformational switch in the multidrug transporter LmrP.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Protonation drives the conformational switch in the multidrug transporter LmrP.
@ast
Protonation drives the conformational switch in the multidrug transporter LmrP.
@en
type
label
Protonation drives the conformational switch in the multidrug transporter LmrP.
@ast
Protonation drives the conformational switch in the multidrug transporter LmrP.
@en
prefLabel
Protonation drives the conformational switch in the multidrug transporter LmrP.
@ast
Protonation drives the conformational switch in the multidrug transporter LmrP.
@en
P2093
P2860
P356
P1476
Protonation drives the conformational switch in the multidrug transporter LmrP.
@en
P2093
Chloé Martens
Cédric Govaerts
Hassane S Mchaourab
Jean-Marie Ruysschaert
Matthieu Masureel
Richard A Stein
Smriti Mishra
P2860
P2888
P304
P356
10.1038/NCHEMBIO.1408
P577
2013-12-08T00:00:00Z