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  Crystal structure and mechanistic basis of a functional homolog of the antigen transporter TAP

Nöll, A., Christoph, T., Herbring, V., Zollmann, T., Barth, K., Mehdipour, A. R., et al. (2017). Crystal structure and mechanistic basis of a functional homolog of the antigen transporter TAP. Proceedings of the National Academy of Sciences of the United States of America, 114(4), E438-E447. doi:10.1073/pnas.1620009114.

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Nöll, Anne1, Autor
Christoph, Thomas1, Autor
Herbring, Valentina1, Autor
Zollmann, Tina1, Autor
Barth, Katja1, 2, Autor
Mehdipour, Ahmad Reza3, Autor           
Tomasiak, Thomas M.4, Autor
Brüchert, Stefan1, Autor
Joseph, Benesh2, Autor
Abele, Rupert1, Autor
Oliéric, Vincent5, Autor
Wang, Meitian5, Autor
Diederichs, Kay6, Autor
Hummer, Gerhard3, 7, Autor                 
Stroud, Robert M.4, Autor
Pos, Klaas M.1, Autor
Tampé, Robert1, Autor
Affiliations:
1Institute of Biochemistry, Biocenter, Goethe University Frankfurt, 60438 Frankfurt am Main, Germany, ou_persistent22              
2Institute of Physical and Theoretical Chemistry, Goethe University Frankfurt, 60438 Frankfurt am Main, Germany, ou_persistent22              
3Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
4Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94158, ou_persistent22              
5Swiss Light Source, Paul Scherrer Institute, 5232 Villigen PSI, Switzerland, ou_persistent22              
6Molecular Bioinformatics, Department of Biology, University of Konstanz, 78457 Konstanz, Germany, ou_persistent22              
7Institute of Biophysics, Goethe University Frankfurt, 60438 Frankfurt am Main, Germany, ou_persistent22              

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Schlagwörter: ABC transporter; conformational dynamics; membrane proteins; peptide transport; transporter associated with antigen processing
 Zusammenfassung: ABC transporters form one of the largest protein superfamilies in all domains of life, catalyzing the movement of diverse substrates across membranes. In this key position, ABC transporters can mediate multidrug resistance in cancer therapy and their dysfunction is linked to various diseases. Here, we describe the 2.7-Å X-ray structure of heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), which not only shares structural homology with the antigen translocation complex TAP, but is also able to restore antigen processing in human TAP-deficient cells. TmrAB exhibits a broad peptide specificity and can concentrate substrates several thousandfold, using only one single active ATP-binding site. In our structure, TmrAB adopts an asymmetric inward-facing state, and we show that the C-terminal helices, arranged in a zipper-like fashion, play a crucial role in guiding the conformational changes associated with substrate transport. In conclusion, TmrAB can be regarded as a model system for asymmetric ABC exporters in general, and for TAP in particular.

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Sprache(n): eng - English
 Datum: 2017-01-092017-01-24
 Publikationsstatus: Erschienen
 Seiten: 10
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1073/pnas.1620009114
 Art des Abschluß: -

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Titel: Proceedings of the National Academy of Sciences of the United States of America
  Andere : Proceedings of the National Academy of Sciences of the USA
  Andere : Proc. Acad. Sci. USA
  Andere : Proc. Acad. Sci. U.S.A.
  Kurztitel : PNAS
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Washington, D.C. : National Academy of Sciences
Seiten: - Band / Heft: 114 (4) Artikelnummer: - Start- / Endseite: E438 - E447 Identifikator: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230