NDLI: Role of the two structural domains from the periplasmic Escherichia coli histidine-binding protein HisJ.

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Role of the two structural domains from the periplasmic Escherichia coli histidine-binding protein HisJ.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Chu, Byron C. H. Dewolf, Timothy Vogel, Hans J.
Description	Author Affiliation: Chu BC ( From the Biochemistry Research Group, Department of Biological Sciences, University of Calgary, Alberta T2N 1N4, Canada.)
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.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	44
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Escherichia Coli K12 Chemistry Escherichia Coli Proteins Histidine Periplasmic Binding Proteins Genetics Metabolism Ligands Nuclear Magnetic Resonance, Biomolecular Protein Binding Protein Structure, Tertiary Structural Homology, Protein Structure-Activity Relationship Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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