Conformational dynamics of the ABC transporter McjD seen by single-molecule FRET (216 views)
The Embo J, 2018 Nov; 2;37(21): N/D-N/D.
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Paper type: Journal Article,
Impact factor: 9.96, 5-year impact factor: 8.63
Url: https://www.embopress.org/doi/full/10.15252/embj.2018100056
Keywords: Abc Transporter, Mcjd, Smfret, Atp Binding Cassette,
Affiliations:
*** IBB - CNR ***
Molecular Microscopy Research Group, Zernike Institute for Advanced Materials, University of Groningen, Groningen, The Netherlands.
Department of Life Sciences, Imperial College London, London, UK.
Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot, UK.
Communication Molecules and Adaptation of Microorganisms Laboratory, (MCAM, UMR 7245 CNRS-MNHN), Muséum National d'Histoire Naturelle, Centre National de la Recherche Scientifique, Sorbonne Universités, Paris, France.
Physical and Synthetic Biology, Faculty of Biology, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany.
References:
Not available.
The Embo J, 2018 Nov; 2;37(21): N/D-N/D.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 9.96, 5-year impact factor: 8.63
Url: https://www.embopress.org/doi/full/10.15252/embj.2018100056
Keywords: Abc Transporter, Mcjd, Smfret, Atp Binding Cassette,
Affiliations:
*** IBB - CNR ***
Molecular Microscopy Research Group, Zernike Institute for Advanced Materials, University of Groningen, Groningen, The Netherlands.
Department of Life Sciences, Imperial College London, London, UK.
Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot, UK.
Communication Molecules and Adaptation of Microorganisms Laboratory, (MCAM, UMR 7245 CNRS-MNHN), Muséum National d'Histoire Naturelle, Centre National de la Recherche Scientifique, Sorbonne Universités, Paris, France.
Physical and Synthetic Biology, Faculty of Biology, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany.
References:
Not available.
Conformational dynamics of the ABC transporter McjD seen by single-molecule FRET
ABC transporters utilize ATP for export processes to provide cellular resistance against toxins, antibiotics, and harmful metabolites in eukaryotes and prokaryotes. Based on static structure snapshots, it is believed that they use an alternating access mechanism, which couples conformational changes to ATP binding (outward-open conformation) and hydrolysis (inward-open) for unidirectional transport driven by ATP Here, we analyzed the conformational states and dynamics of the antibacterial peptide exporter McjD from Escherichia coli using single-molecule Förster resonance energy transfer (smFRET). For the first time, we established smFRET for an ABC exporter in a native-like lipid environment and directly monitor conformational dynamics in both the transmembrane- (TMD) and nucleotide-binding domains (NBD). With this, we unravel the ligand dependences that drive conformational changes in both domains. Furthermore, we observe intrinsic conformational dynamics in the absence of ATP and ligand in the NBDs. ATP binding and hydrolysis on the other hand can be observed via NBD conformational dynamics. We believe that the progress made here in combination with future studies will facilitate full understanding of ABC transport cycles.
ABC transporters utilize ATP for export processes to provide cellular resistance against toxins, antibiotics, and harmful metabolites in eukaryotes and prokaryotes. Based on static structure snapshots, it is believed that they use an alternating access mechanism, which couples conformational changes to ATP binding (outward-open conformation) and hydrolysis (inward-open) for unidirectional transport driven by ATP Here, we analyzed the conformational states and dynamics of the antibacterial peptide exporter McjD from Escherichia coli using single-molecule Förster resonance energy transfer (smFRET). For the first time, we established smFRET for an ABC exporter in a native-like lipid environment and directly monitor conformational dynamics in both the transmembrane- (TMD) and nucleotide-binding domains (NBD). With this, we unravel the ligand dependences that drive conformational changes in both domains. Furthermore, we observe intrinsic conformational dynamics in the absence of ATP and ligand in the NBDs. ATP binding and hydrolysis on the other hand can be observed via NBD conformational dynamics. We believe that the progress made here in combination with future studies will facilitate full understanding of ABC transport cycles.
Conformational dynamics of the ABC transporter McjD seen by single-molecule FRET
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Conformational dynamics of the ABC transporter McjD seen by single-molecule FRET
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* Structural Basis for Natural Product Selection and Export by Bacterial ABC Transporters (241 views)
Acs Chemical Biology, 2018 Jun; 13(6): 1598-1609.
Impact Factor: 4.374
View Export to BibTeX Export to EndNote
Ruggiero A, Dattelbaum JD, Staiano M, Berisio R, D'Auria S, Vitagliano L
* A loose domain swapping organization confers a remarkable stability to the dimeric structure of the arginine binding protein from Thermotoga maritima (696 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2014 May 15; 9(5): e96560-e96560.
Impact Factor: 3.234
View Export to BibTeX Export to EndNote
Del Vecchio S, Zannetti A, Fonti R, Iommelli F, Lettieri A, Salvatore M
* Molecular imaging of drug resistance in cancer (506 views)
Minerva Biotecnol (ISSN: 1120-4826), 2009 Mar; 21(1): 31-36.
Impact Factor: 0.268
View Export to BibTeX Export to EndNote
Del Vecchio S, Salvatore M
* Tc-99m-MIBI in the evaluation of breast cancer biology (715 views) (PDF 198 views)
Eur J Nucl Med (ISSN: 1619-7070, 1619-7089, 0340-6997), 2004 Jun; 31(SUPPL.1): S88-S88.
Impact Factor: 3.935
View Export to BibTeX Export to EndNote
4 Records (3 excluding Abstracts).
Total impact factor: 11.811 (7.876 excluding Abstracts).
Total 5 year impact factor: 13.712 (8.984 excluding Abstracts).
Total impact factor: 11.811 (7.876 excluding Abstracts).
Total 5 year impact factor: 13.712 (8.984 excluding Abstracts).
216 views. Last view on Monday 07 October 2024, 8:52:03
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