NMR localization of the O-mycoloylation on PorH, a channel forming peptide from Corynebacterium glutamicum.
 

NMR localization of the O-mycoloylation on PorH, a channel forming peptide from Corynebacterium glutamicum.

http://www.bionmr.com//www.ncbi.nlm....PubMedLink.gif Related Articles NMR localization of the O-mycoloylation on PorH, a channel forming peptide from Corynebacterium glutamicum.

FEBS Lett. 2013 Nov 15;587(22):3687-91

Authors: Rath P, Saurel O, Tropis M, Daffé M, Demange P, Milon A

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.


PMID: 24100136 [PubMed - indexed for MEDLINE]



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