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Oligomeric structure of the carnitine transporter CaiT from Escherichia coli.
Vinothkumar KR, Raunser S, Jung H, Kühlbrandt W. Vinothkumar KR, et al. Among authors: jung h. J Biol Chem. 2006 Feb 24;281(8):4795-801. doi: 10.1074/jbc.M508993200. Epub 2005 Dec 19. J Biol Chem. 2006. PMID: 16365043 Free article.
Unlike the other members of this transporter family, it does not require an ion gradient and does not respond to osmotic stress (Jung, H., Buchholz, M., Clausen, J., Nietschke, M., Revermann, A., Schmid, R., and Jung, K. (2002) J. ...
Unlike the other members of this transporter family, it does not require an ion gradient and does not respond to osmotic stress (Jung …
Transmembrane domain II of the Na+/proline transporter PutP of Escherichia coli forms part of a conformationally flexible, cytoplasmic exposed aqueous cavity within the membrane.
Pirch T, Landmeier S, Jung H. Pirch T, et al. Among authors: jung h. J Biol Chem. 2003 Oct 31;278(44):42942-9. doi: 10.1074/jbc.M308253200. Epub 2003 Aug 15. J Biol Chem. 2003. PMID: 12923181 Free article.
Previous work on PutP suggests an involvement of the region ranging from Asp-55 to Gly-58 in binding of Na+ and/or proline (Pirch, T., Quick, M., Nietschke, M., Langkamp, M., Jung, H. (2002) J. Biol. Chem. 277, 8790-8796). In this study, a complete Cys scanning muta …
Previous work on PutP suggests an involvement of the region ranging from Asp-55 to Gly-58 in binding of Na+ and/or proline (Pirch, T., Quick …
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