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  Structural and Functional Fingerprint of the Mitochondrial ATP-binding Cassette Transporter Mdl1 from Saccharomyces cerevisiae

Hofacker, M., Gompf, S., Zutz, A., Presenti, C., Haase, W., van der Does, C., et al. (2007). Structural and Functional Fingerprint of the Mitochondrial ATP-binding Cassette Transporter Mdl1 from Saccharomyces cerevisiae. The Journal of Biological Chemistry, 282(6), 3951-3961. doi:10.1074/jbc.M609899200.

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 Urheber:
Hofacker, Matthias1, Autor
Gompf, Simone1, Autor
Zutz, Ariane1, Autor
Presenti, Chiara1, Autor
Haase, Winfried2, Autor           
van der Does, Chris1, Autor
Model, Kirstin2, 3, Autor           
Tampé, Robert1, Autor
Affiliations:
1Institute of Biochemistry, Biocenter, Johann Wolfgang Goethe University, 60438 Frankfurt am Main, Germany, ou_persistent22              
2Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
3MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, United Kingdom, ou_persistent22              

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 Zusammenfassung: The ATP-binding cassette half-transporter Mdl1 from Saccharomyces cerevisiae has been proposed to be involved in the quality control of misassembled respiratory chain complexes by exporting degradation products generated by the m-AAA proteases from the matrix. Direct functional or structural data of the transport complex are, however, not known so far. After screening expression in various hosts, Mdl1 was overexpressed 100-fold to 1% of total mitochondrial membrane protein in S. cerevisiae. Based on detergent screens, Mdl1 was solubilized and purified to homogeneity. Mdl1 showed a high binding affinity for MgATP (Kd = 0.26 μm) and an ATPase activity with a Km of 0.86 mm (Hill coefficient of 0.98) and a turnover rate of 2.6 ATP/s. Mutagenesis of the conserved glutamate downstream of the Walker B motif (E599Q) or the conserved histidine of the H-loop (H631A) abolished ATP hydrolysis, whereas ATP binding was not affected. Mdl1 reconstituted into liposomes showed an ATPase activity similar to the solubilized complex. By single particle electron microscopy, a first three-dimensional structure of the mitochondrial ATP-binding cassette transporter was derived at 2.3-nm resolution, revealing a homodimeric complex in an open conformation.

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Sprache(n): eng - English
 Datum: 2006-12-052006-10-232006-12-062007-02-09
 Publikationsstatus: Erschienen
 Seiten: 11
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1074/jbc.M609899200
PMID: 17150958
 Art des Abschluß: -

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Titel: The Journal of Biological Chemistry
  Andere : JBC
  Kurztitel : J. Biol. Chem.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Seiten: - Band / Heft: 282 (6) Artikelnummer: - Start- / Endseite: 3951 - 3961 Identifikator: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1