Ligand-specific opening of a gated-porin channel in the outer membrane of living bacteria

Ligand-specific opening of a gated-porin channel in the outer membrane of living bacteria

Autor Jiang, X. Q. Google Scholar
Payne, M. A. Google Scholar
Cao, Z. H. Google Scholar
Foster, S. B. Google Scholar
Feix, J. B. Google Scholar
Newton, SMC Google Scholar
Klebba, P. E. Google Scholar
Universidade Federal de São Paulo (UNIFESP)
Resumo Ligand-gated membrane channels selectively facilitate the entry of iron into prokaryotic cells. the essential role of iron in metabolism makes its acquisition a determinant of bacterial pathogenesis and a target for therapeutic strategies. in Gram-negative bacteria, TonB-dependent outer membrane proteins form energized, gated pores that bind iron chelates (siderophores) and internalize them. the time-resolved operation of the Escherichia coli ferric enterobactin receptor FepA was observed in vivo with electron spin resonance spectroscopy by monitoring the mobility of covalently bound nitroxide spin labels. A ligand-binding surface loop of FepA, which normally closes its transmembrane channel, exhibited energy-dependent structural changes during iron and toxin (colicin) transport. These changes were not merely associated with ligand binding, but occurred during ligand uptake through the outer membrane bilayer. the results demonstrate by a physical method that gated-porin channels open and close during membrane transport in vivo.
Idioma Inglês
Data 1997-05-23
Publicado em Science. Washington: Amer Assoc Advancement Science, v. 276, n. 5316, p. 1261-1264, 1997.
ISSN 0036-8075 (Sherpa/Romeo, fator de impacto)
Editor Amer Assoc Advancement Science
Extensão 1261-1264
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:A1997XA49700045

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