Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870820 | FEBS Letters | 2013 | 5 Pages |
Abstract
PorH and PorA are two small peptides that, in complex, form a voltage-dependent ion channel in the outer membrane of Corynebacterium glutamicum. Specific post-translational modifications on PorA and PorH are required for the formation of a functional ion channel. The assignment of PorH proton NMR chemical shifts in DMSO, allowed identifying unambiguously the exact position of the PorH O-mycoloylation on Ser 56 side chain. This was further confirmed by site directed mutagenesis and mass spectrometry. Together with the previously published localization of PorA mycoloylation, this provides the complete primary structure characterization of this outer membrane porin.
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Authors
Parthasarathi Rath, Olivier Saurel, Maryelle Tropis, Mamadou Daffé, Pascal Demange, Alain Milon,