which biomolecule as selective affinity to histidine and attaches to it through non-covalent bonds
the bacterial periplasmic histidine-binding proteins (hisj) can function in histidine transport. The significance of this interaction involves the selective transport of histidine. The structure is bi-lobate; the two lobes, one bigger than the other, are connected by two short strands and are in contact with each other (closed) enclosing the histidine. Charged, polar, and non-polar side chains, as well as the peptide backbone, are involved in tight binding of the histidine. The bound histidine is involved in eight direct hydrogen bonds, six with the bigger lobe and two with the smaller lobe, in one potential water-mediated hydrogen bond with the bigger lobe, as well as in ionic interactions.
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