ArticlePloS one2014
The crystal structures of apo and cAMP-bound GlxR from Corynebacterium glutamicum reveal structural and dynamic changes upon cAMP binding in CRP/FNR family transcription factors.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed.
- Sequence-encoded dynamics diversify allostery within a conserved protein scaffold.Protein science : a publication of the Protein Society · 2026Article
- High-throughput investigation of macromolecular interactions for drug development using spectral shift technology.Biophysical reviews · 2025Review
- Structures of the cyanobacterial nitrogen regulators NtcA and PipX complexed to DNA shed light on DNA binding by NtcA and implicate PipX in the recruitment of RNA polymerase.Nucleic acids research · 2025Article
- The cAMP receptor protein from Gardnerella vaginalis is not regulated by ligands.Communications biology · 2024Article
- Article
- Structural and functional diversity of bacterial cyclic nucleotide perception by CRP proteins.microLife · 2023Review
- Global Regulator of Rubber Degradation in Gordonia polyisoprenivorans VH2: Identification and Involvement in the Regulation Network.Applied and environmental microbiology · 2020Article
- Essential site scanning analysis: A new approach for detecting sites that modulate the dispersion of protein global motions.Computational and structural biotechnology journal · 2020Article
- Molecular Basis of Growth Inhibition by Acetate of an Adenylate Cyclase-Deficient Mutant ofFrontiers in microbiology · 2020Article
- Nucleotide signaling pathway convergence in a cAMP-sensing bacterial c-di-GMP phosphodiesterase.The EMBO journal · 2019Article
- Novel structural features drive DNA binding properties of Cmr, a CRP family protein in TB complex mycobacteria.Nucleic acids research · 2018Article
- Directed evolution of the Escherichia coli cAMP receptor protein at the cAMP pocket.The Journal of biological chemistry · 2015Article
- Dynamic Transmission of Protein Allostery without Structural Change: Spatial Pathways or Global Modes?Biophysical journal · 2015Article
- Regulation of the pstSCAB operon in Corynebacterium glutamicum by the regulator of acetate metabolism RamB.BMC microbiology · 2015Article
- Global low-frequency motions in protein allostery: CAP as a model system.Biophysical reviewsArticle
- cAMP is an allosteric modulator of DNA-binding specificity in the cAMP receptor protein from Mycobacterium tuberculosis.The Journal of biological chemistryArticle
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11 authors.
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Abstract
The cyclic AMP-dependent transcriptional regulator GlxR from Corynebacterium glutamicum is a member of the super-family of CRP/FNR (cyclic AMP receptor protein/fumarate and nitrate reduction regulator) transcriptional regulators that play central roles in bacterial metabolic regulatory networks. In C. glutamicum, which is widely used for the industrial production of amino acids and serves as a non-pathogenic model organism for members of the Corynebacteriales including Mycobacterium tuberculosis, the GlxR homodimer controls the transcription of a large number of genes involved in carbon metabolism. GlxR therefore represents a key target for understanding the regulation and coordination of C. glutamicum metabolism. Here we investigate cylic AMP and DNA binding of GlxR from C. glutamicum and describe the crystal structures of apo GlxR determined at a resolution of 2.5 Å, and two crystal forms of holo GlxR at resolutions of 2.38 and 1.82 Å, respectively. The detailed structural analysis and comparison of GlxR with CRP reveals that the protein undergoes a distinctive conformational change upon cyclic AMP binding leading to a dimer structure more compatible to DNA-binding. As the two binding sites in the GlxR homodimer are structurally identical dynamic changes upon binding of the first ligand are responsible for the allosteric behavior. The results presented here show how dynamic and structural changes in GlxR lead to optimization of orientation and distance of its two DNA-binding helices for optimal DNA recognition.
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