The ABC transporter MsbA plays a critical role in Gram-negative bacteria in the regulation of the outer membrane by translocating core-LPS across the inner membrane. Additionally, a broad substrate specificity for lipophilic drugs has been shown. The allosteric interplay between substrate binding in the transmembrane domains and ATP binding and turnover in the nucleotide-binding domains must be mediated via the NBD/TMD interface. Previous studies suggested the involvement of two intracellular...
[ASAP] Solid-State NMR Reveals Asymmetric ATP Hydrolysis in the Multidrug ABC Transporter BmrA
Solid-State NMR Reveals Asymmetric ATP Hydrolysis in the Multidrug ABC Transporter BmrA
Denis Lacabanne, Thomas Wiegand, Margot Di Cesare, Ce?dric Orelle, Matthias Ernst, Jean-Michel Jault, Beat H. Meier, and Anja Bo?ckmann
https://pubs.acs.org/cms/10.1021/jacs.2c04287/asset/images/medium/ja2c04287_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.2c04287
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[NMR paper] Solid-state NMR 13C and 15*N resonance assignments of Vibrio sp. SemiSWEET transporter in lipid bilayers
Solid-state NMR 13C and 15*N resonance assignments of Vibrio sp. SemiSWEET transporter in lipid bilayers
The Sugar Will Eventually be Exported Transporter (SWEET) family is a new class of transporters that plays crucial roles in the cellular sugar transport process. Their bacterial homologs, known as SemiSWEETs, are among the smallest transporters and can be used as a prototype for studying the biological properties of sugar transporters. Here, a set of dipolar-based multidimensional solid-state NMR spectra were employed to investigate the structure of Vibrio sp. SemiSWEET...
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07-01-2022 10:59 AM
[NMR paper] Probing allosteric coupling in a constitutively open mutant of the ion channel KcsA using solid-state NMR.
Probing allosteric coupling in a constitutively open mutant of the ion channel KcsA using solid-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full.gif Related Articles Probing allosteric coupling in a constitutively open mutant of the ion channel KcsA using solid-state NMR.
Proc Natl Acad Sci U S A. 2020 03 31;117(13):7171-7175
Authors: Sun Z, Xu Y, Zhang D, McDermott AE
Abstract
Transmembrane allosteric coupling is a feature of...
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07-18-2020 10:53 AM
Probing allosteric coupling in a constitutively open mutant of the ion channel KcsA using solid-state NMR [Biophysics and Computational Biology]
Probing allosteric coupling in a constitutively open mutant of the ion channel KcsA using solid-state NMR
Zhiyu Sun, Yunyao Xu, Dongyu Zhang, Ann E. McDermott...
Date: 2020-03-31
Transmembrane allosteric coupling is a feature of many critical biological signaling events. Here we test whether transmembrane allosteric coupling controls the potassium binding affinity of the prototypical potassium channel KcsA in the context of C-type inactivation. Activation of KcsA is initiated by proton binding to the pH gate upon an... Read More
PNAS:
Number: 13
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[NMR paper] The effect of drug binding on specific sites in transmembrane helices 4 and 6 of the ABC exporter MsbA studied by DNP-enhanced solid-state NMR.
The effect of drug binding on specific sites in transmembrane helices 4 and 6 of the ABC exporter MsbA studied by DNP-enhanced solid-state NMR.
Related Articles The effect of drug binding on specific sites in transmembrane helices 4 and 6 of the ABC exporter MsbA studied by DNP-enhanced solid-state NMR.
Biochim Biophys Acta. 2017 Oct 22;:
Authors: Spadaccini R, Kaur H, Becker-Baldus J, Glaubitz C
Abstract
MsbA, a homodimeric ABC exporter, translocates its native substrate lipid A as well as a range of smaller, amphiphilic...
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10-28-2017 08:03 AM
[NMR paper] Antigenic peptide recognition on the human ABC transporter TAP resolved by DNP-enhanced solid-state NMR spectroscopy.
Antigenic peptide recognition on the human ABC transporter TAP resolved by DNP-enhanced solid-state NMR spectroscopy.
Related Articles Antigenic peptide recognition on the human ABC transporter TAP resolved by DNP-enhanced solid-state NMR spectroscopy.
J Am Chem Soc. 2016 Sep 23;
Authors: Lehnert E, Mao J, Mehdipour AR, Hummer G, Abele R, Glaubitz C, Tampé R
Abstract
The human transporter associated with antigen processing (TAP) is a 140-kDa heterodimeric ABC transport complex, which selects peptides for export into the...
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09-24-2016 05:20 PM
[NMR paper] The ABC exporter MsbA probed by solid state NMR - challenges and opportunities.
The ABC exporter MsbA probed by solid state NMR - challenges and opportunities.
Related Articles The ABC exporter MsbA probed by solid state NMR - challenges and opportunities.
Biol Chem. 2015 Apr 4;
Authors: Kaur H, Lakatos A, Spadaccini R, Vogel R, Hoffmann C, Becker-Baldus J, Ouari O, Tordo P, Mchaourab H, Glaubitz C
Abstract
ABC transporters form a superfamily of integral membrane proteins involved in translocation of substrates across the membrane driven by ATP hydrolysis. Despite available crystal structures and extensive...
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04-09-2015 03:47 AM
[NMR paper] Ligand-Induced Conformational Changes of the Multidrug Resistance Transporter EmrE Probed by Oriented Solid-State NMR Spectroscopy.
Ligand-Induced Conformational Changes of the Multidrug Resistance Transporter EmrE Probed by Oriented Solid-State NMR Spectroscopy.
Ligand-Induced Conformational Changes of the Multidrug Resistance Transporter EmrE Probed by Oriented Solid-State NMR Spectroscopy.
Angew Chem Int Ed Engl. 2013 Aug 12;
Authors: Gayen A, Banigan JR, Traaseth NJ
Abstract
An EmrE-ging market: Oriented solid-state NMR spectroscopy and biochemical cross-linking experiments were used to show that the ligand-free membrane protein transporter EmrE forms...
Probing the allosteric NBD-TMD crosstalk in the ABC transporter MsbA by solid-state NMR
Linear Mode
