ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2007
Conformational studies of the manganese transport regulator (MntR) from Bacillus subtilis using deuterium exchange mass spectrometry.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2007. 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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15 citing papers in PubMed, 24 citations in OpenAlex.
- Structural Dynamics of theInternational journal of molecular sciences · 2023Article
- Genetic Regulation of Metal Ion Homeostasis in Staphylococcus aureus.Trends in microbiology · 2020Review
- Allosteric control of metal-responsive transcriptional regulators in bacteria.The Journal of biological chemistry · 2020Review
- Metallochaperones and metalloregulation in bacteria.Essays in biochemistry · 2017Review
- Characterisation of the Porphyromonas gingivalis Manganese Transport Regulator Orthologue.PloS one · 2016Article
- Co(2+)-dependent gene expression in Streptococcus pneumoniae: opposite effect of Mn(2+) and Co(2+) on the expression of the virulence genes psaBCA, pcpA, and prtA.Frontiers in microbiology · 2015Article
- Physical characterization of the manganese-sensing pneumococcal surface antigen repressor from Streptococcus pneumoniae.Biochemistry · 2013Article
- Roles of the A and C sites in the manganese-specific activation of MntR.Biochemistry · 2013Article
- Regulating SR protein phosphorylation through regions outside the kinase domain of SRPK1.Journal of molecular biology · 2011Article
- Metalloregulatory proteins: metal selectivity and allosteric switching.Biophysical chemistry · 2011Review
- Mechanism of substrate specificity in 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases.Journal of structural biology · 2011Article
- The metalloregulatory zinc site in Streptococcus pneumoniae AdcR, a zinc-activated MarR family repressor.Journal of molecular biology · 2010Article
- Energetics of allosteric negative coupling in the zinc sensor S. aureus CzrA.Journal of the American Chemical Society · 2009Article
- Coordination chemistry of bacterial metal transport and sensing.Chemical reviews · 2009Review
- Pro-interleukin (IL)-1beta shares a core region of stability as compared with mature IL-1beta while maintaining a distinctly different configurational landscape: a comparative hydrogen/deuterium exchange mass spectrometry study.The Journal of biological chemistry · 2009Article
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4 authors at 1 institution in 1 country.
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Abstract
The manganese transport regulator (MntR) of Bacillus subtilis is a metalloregulatory protein responsible for regulation of genes involved in manganese uptake by this organism. MntR belongs to the iron-responsive DtxR family, but is allosterically regulated by manganese and cadmium ions. Having previously characterized the metal binding affinities of this protein as well as the DNA-binding activation profiles for the relevant metal ions, we have focused the current study on investigating the structural changes of MntR in solution upon binding divalent transition metal ions. Deuterium exchange mass spectrometry was utilized to investigate the deuterium exchange dynamics between apo-MntR, Co(2+)-MntR, Cd(2+)-MntR, and Mn(2+)-MntR. Comparing the rates of deuteration of each metal-bound form of MntR reveals that the N-terminal DNA-binding motif is more mobile in solution than the C-terminal dimerization domain. Furthermore, significant protection from deuterium exchange is observed in the helices that contribute metal-chelating amino acids to form the metal binding site of MntR. In contrast, the bulk of the DNA-binding winged helix-turn-helix motif shows no difference in deuterium exchange upon metal binding. Mapping of the deuteration patterns onto the crystal structures of MntR yields insight into how metal binding affects the protein structure and complements earlier studies on the mechanism of MntR. Metal binding acts to rigidify MntR, thereby limiting the mobility of the protein and reducing the entropic cost of DNA binding.
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