Characterization of the protonation and hydrogen bonding state of the histidine residues in IIAmtl, a domain of the phosphoenolpyruvate-dependent mannitol-specific transport protein

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Abstract
The A domain of the mannitol-specific EII, IIAmtl, was subcloned and proven to be functional in the isolated form. It contains a histidine phosphorylation site, the first of two phosphorylation sites in the parent protein. In this paper, we describe the characterization of the three histidine residues in IIAmtl with respect to their protonation and hydrogen bonding state, using 1H{15N} heteronuclear NMR techniques and protein selectively enriched with [δ1,ε2-15N] histidine. The active site residue has a low pKa

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