ArticleProtein science : a publication of the Protein Society2017
Ligand binding specificity of the Escherichia coli periplasmic histidine binding protein, HisJ.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed.
- Characterization of Cationic Amino Acid Binding Protein from Candidatus Liberibacter Asiaticus and in Silico Study to Identify Potential Inhibitor Molecules.The protein journal · 2024Article
- In vitro antimicrobial, anticancer evaluation, and in silico studies of mannopyranoside analogs against bacterial and fungal proteins: Acylation leads to improved antimicrobial activity.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2024Article
- Multi-Omics ofMicroorganisms · 2024Article
- Revealing Allosteric Mechanism of Amino Acid Binding Proteins from Open to Closed State.Molecules (Basel, Switzerland) · 2023Article
- Biochemical studies highlight determinants for metal selectivity in the Escherichia coli periplasmic solute binding protein NikA.Metallomics : integrated biometal science · 2022Article
- The measurement of binding affinities by NMR chemical shift perturbation.Journal of biomolecular NMR · 2022Article
- Investigating the roles of the conserved CuJournal of inorganic biochemistry · 2020Article
- Article
- Substrate recognition and ATPase activity of theThe Journal of biological chemistry · 2020Article
- Structure dictates the mechanism of ligand recognition in the histidine and maltose binding proteins.Current research in structural biology · 2020Article
- Homology modeling identified for purported drug targets to the neuroprotective effects of levodopa and asiaticoside-D in degenerated cerebral ganglions ofIndian journal of pharmacologyArticle
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Abstract
The HisJ protein from Escherichia coli and related Gram negative bacteria is the periplasmic component of a bacterial ATP-cassette (ABC) transporter system. Together these proteins form a transmembrane complex that can take up L-histidine from the environment and translocate it into the cytosol. We have studied the specificity of HisJ for binding L-His and many related naturally occurring compounds. Our data confirm that L-His is the preferred ligand, but that 1-methyl-L-His and 3-methyl-L-His can also bind, while the dipeptide carnosine binds weakly and D-histidine and the histidine degradation products, histamine, urocanic acid and imidazole do not bind. L-Arg, homo-L-Arg, and post-translationally modified methylated Arg-analogs also bind with reasonable avidity, with the exception of symmetric dimethylated-L-Arg. In contrast, L-Lys and L-Orn have considerably weaker interactions with HisJ and methylated and acetylated Lys variants show relatively poor binding. It was also observed that the carboxylate group of these amino acids and their variants was very important for proper recognition of the ligand. Taken together our results are a key step towards designing HisJ as a specific protein-based reagentless biosensor.
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