ArticleThe Journal of biological chemistry2013
Role of the two structural domains from the periplasmic Escherichia coli histidine-binding protein HisJ.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- CH•••S hydrogen bonds drive molecular recognition of ergothioneine by the microbial transporter.Science advances · 2026Article
- Expression, purification, and characterization of diacylated Lipo-YcjN frombioRxiv : the preprint server for biology · 2024Article
- Retracing the evolution of a modern periplasmic binding protein.Protein science : a publication of the Protein Society · 2023Article
- Revealing Allosteric Mechanism of Amino Acid Binding Proteins from Open to Closed State.Molecules (Basel, Switzerland) · 2023Article
- Discovery and structure of a widespread bacterial ABC transporter specific for ergothioneine.Nature communications · 2022Article
- Altered conformational sampling along an evolutionary trajectory changes the catalytic activity of an enzyme.Nature communications · 2020Article
- Article
- Structure dictates the mechanism of ligand recognition in the histidine and maltose binding proteins.Current research in structural biology · 2020Article
- NMR Analysis of Apo Glutamine-Binding Protein Exposes Challenges in the Study of Interdomain Dynamics.Angewandte Chemie (International ed. in English) · 2019Article
- Expression and Purification of Chemokine MIP-3α (CCL20) through a Calmodulin-Fusion Protein System.Microorganisms · 2019Article
- A genetically encoded toolkit for tracking live-cell histidine dynamics in space and time.Scientific reports · 2017Article
- Ligand binding specificity of the Escherichia coli periplasmic histidine binding protein, HisJ.Protein science : a publication of the Protein Society · 2017Article
- Role of cis-trans proline isomerization in the function of pathogenic enterobacterial Periplasmic Binding Proteins.PloS one · 2017Article
- Pulse EPR-enabled interpretation of scarce pseudocontact shifts induced by lanthanide binding tags.Journal of biomolecular NMR · 2016Article
- The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepB.The Journal of biological chemistry · 2014Article
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3 authors.
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Abstract
Escherichia coli HisJ is a type II periplasmic binding protein that functions to reversibly capture histidine and transfer it to its cognate inner membrane ABC permease. Here, we used NMR spectroscopy to determine the structure of apo-HisJ (26.5 kDa) in solution. HisJ is a bilobal protein in which domain 1 (D1) is made up of two noncontiguous subdomains, and domain 2 (D2) is expressed as the inner domain. To better understand the roles of D1 and D2, we have isolated and characterized each domain separately. Structurally, D1 closely resembles its homologous domain in apo- and holo-HisJ, whereas D2 is more similar to the holo-form. NMR relaxation experiments reveal that HisJ becomes more ordered upon ligand binding, whereas isolated D2 experiences a significant reduction in slower (millisecond to microsecond) motions compared with the homologous domain in apo-HisJ. NMR titrations reveal that D1 is able to bind histidine in a similar manner as full-length HisJ, albeit with lower affinity. Unexpectedly, isolated D1 and D2 do not interact with each other in the presence or absence of histidine, which indicates the importance of intact interdomain-connecting elements (i.e. hinge regions) for HisJ functioning. Our results shed light on the binding mechanism of type II periplasmic binding proteins where ligand is initially bound by D1, and D2 plays a supporting role in this dynamic process.
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