The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric.
about
Analyzing conformational changes in the transport cycle of EmrEIntrinsic conformational plasticity of native EmrE provides a pathway for multidrug resistanceA structured loop modulates coupling between the substrate-binding and dimerization domains in the multidrug resistance transporter EmrE.Combination of ¹⁵N reverse labeling and afterglow spectroscopy for assigning membrane protein spectra by magic-angle-spinning solid-state NMR: application to the multidrug resistance protein EmrEBlocking dynamics of the SMR transporter EmrE impairs efflux activityAntiparallel EmrE exports drugs by exchanging between asymmetric structuresEfficient and stable reconstitution of the ABC transporter BmrA for solid-state NMR studiesAsymmetric protonation of EmrE.Perplexing new insight into the dynamics of the EmrE transporter.Protonation-dependent conformational dynamics of the multidrug transporter EmrE.NMR and EPR studies of membrane transporters.Amino acid composition analysis of secondary transport proteins from Escherichia coli with relation to functional classification, ligand specificity and structure.Ligand-induced conformational changes of the multidrug resistance transporter EmrE probed by oriented solid-state NMR spectroscopy.Caught in the act: ATP hydrolysis of an ABC-multidrug transporter followed by real-time magic angle spinning NMR.Structural and functional comparison of hexahistidine tagged and untagged forms of small multidrug resistance protein, EmrE.New free-exchange model of EmrE transport.Influence of quaternary cation compound on the size of the Escherichia coli small multidrug resistance protein, EmrE.Ermittlung der Konformation von Bacteriorhodopsin-Peptidschleifen in Purpurmembranen durch Festkörper-MAS-NMR-SpektroskopieThe Conformation of Bacteriorhodopsin Loops in Purple Membranes Resolved by Solid-State MAS NMR SpectroscopySmall Multidrug Resistance Efflux Pumps
P2860
Q26829989-34C3F822-CD51-44D7-9A96-B9686DAFD070Q28657903-AE07B3F9-DA90-41D5-A372-91CC427DC023Q30368751-FA26AB0A-7B66-4899-B21A-AE8FABEE2BD3Q30428852-F99697D3-2102-4F7A-A171-ECCFA5D7B865Q34031146-A8AA5A9B-6AD5-4BC1-BE18-F93DE90BB6BAQ34104584-2073E78C-B15D-40E9-A06C-A8FFD4CBB75BQ35596512-CBC7CB4A-8D86-47D3-BE84-3663B3EC0CFFQ36333191-8A0C1FD7-64BD-4185-9363-A8A97ADE1771Q36333218-4DE4F881-3752-4E55-AEE3-6F27F40AD451Q36563374-BED4CCDC-1A78-470D-A1F4-E2B7AB4682B9Q37488240-EE670DFF-1FF9-41EF-8AE3-191227CD6851Q41585383-89EE2FED-33E9-41F0-81CB-7B8BADCBCC30Q42130720-785F1D66-6387-476D-B05A-5D47E08C10CEQ43920815-4A50283A-158E-49ED-B8E4-284FC4B9A79FQ47096111-4BDEEF35-CB4E-4774-A613-702711B47DC8Q47428532-B3DC7905-96EB-42D8-A52D-6DAC17D99E91Q53701129-66DD5B7A-AF6D-4179-A45F-5D67FB990826Q57827792-294A9DD3-E598-4C76-8FFD-29F4430F2B35Q57827804-37F539BA-CD08-431A-817F-C09EF6B8500CQ58023350-9BBF6AC5-80A5-4A8F-9688-08D9D35E82F0
P2860
The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric.
description
2007 nî lūn-bûn
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2007年の論文
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年學術文章
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2007年學術文章
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name
The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric.
@en
The key residue for substrate transport
@nl
type
label
The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric.
@en
The key residue for substrate transport
@nl
prefLabel
The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric.
@en
The key residue for substrate transport
@nl
P2093
P2860
P356
P1476
The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric.
@en
P2093
Bjoern Meyer
Christoph Kaiser
Daniel Basting
Ines Lehner
Michael Karas
Theofanis Manolikas
Winfried Haase
P2860
P304
P356
10.1074/JBC.M707899200
P407
P577
2007-11-27T00:00:00Z