NMR localization of the O-mycoloylation on PorH,a channel forming peptide from Corynebacterium glutamicum |
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Authors: | Parthasarathi Rath,Olivier SaurelMaryelle Tropis,Mamadou Daffé Pascal Demange,Alain Milon |
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Affiliation: | Institute of Pharmacology and Structural Biology, Université de Toulouse, UPS, 205 route de Narbonne, 31077 Toulouse, France; IPBS, UMR 5089, CNRS, 205 route de Narbonne, BP 64182, 31077 Toulouse, France |
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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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Keywords: | Mycolic acid Post translational modification MALDI-TOF Ion channel HSQC-TOCSY HSQC-NOESY |
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