ArticleProtein science : a publication of the Protein Society2006
Structural characterization of GntR/HutC family signaling domain.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Structural and Functional Characterization of Rv0792c from Mycobacterium tuberculosis: Identifying Small Molecule Inhibitor against HutC Protein.Microbiology spectrum · 2023Article
- Global Regulatory Roles of the Histidine-Responsive Transcriptional Repressor HutC in Pseudomonas fluorescens SBW25.Journal of bacteriology · 2020Article
- AFrontiers in cellular and infection microbiology · 2017Article
- Article
- A genomic approach to understand interactions between Streptococcus pneumoniae and its bacteriophages.BMC genomics · 2015Article
- Crystal structure of PhnF, a GntR-family transcriptional regulator of phosphate transport in Mycobacterium smegmatis.Journal of bacteriology · 2014Article
- The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent FAD pyrophosphatase with a potential role in flavin homeostasis.The Journal of biological chemistry · 2013Article
- Characterization of the biocontrol activity of pseudomonas fluorescens strain X reveals novel genes regulated by glucose.PloS one · 2013Article
- Global regulation by the seven-component Pi signaling system.Current opinion in microbiology · 2010Review
- Insight into the induction mechanism of the GntR/HutC bacterial transcription regulator YvoA.Nucleic acids research · 2010Article
- Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of YvoA from Bacillus subtilis.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Structural and functional characterization of the LldR from Corynebacterium glutamicum: a transcriptional repressor involved in L-lactate and sugar utilization.Nucleic acids research · 2008Article
- The carboxyl-terminal domain of TraR, a Streptomyces HutC family repressor, functions in oligomerization.Journal of bacteriology · 2008Article
- Crystal structures of the effector-binding domain of repressor Central glycolytic gene Regulator from Bacillus subtilis reveal ligand-induced structural changes upon binding of several glycolytic intermediates.Molecular microbiology · 2008Article
- Differential regulation of high-affinity phosphate transport systems of Mycobacterium smegmatis: identification of PhnF, a repressor of the phnDCE operon.Journal of bacteriology · 2008Article
- Article
- The structures of transcription factor CGL2947 from Corynebacterium glutamicum in two crystal forms: a novel homodimer assembling and the implication for effector-binding mode.Protein science : a publication of the Protein Society · 2007Article
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Authors and funding
4 authors.
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Abstract
The crystal structure of Escherichia coli PhnF C-terminal domain (C-PhnF) was solved at 1.7 A resolution by the single wavelength anomalous dispersion (SAD) method. The PhnF protein belongs to the HutC subfamily of the large GntR transcriptional regulator family. Members of this family share similar N-terminal DNA-binding domains, but are divided into four subfamilies according to their heterogenic C-terminal domains, which are involved in effector binding and oligomerization. The C-PhnF structure provides for the first time the scaffold of this domain for the HutC subfamily, which covers about 31% of GntR-like regulators. The structure represents a mixture of alpha-helices and beta-strands, with a six-stranded antiparallel beta-sheet at the core. C-PhnF monomers form a dimer by establishing interdomain eight-strand beta-sheets that include core antiparallel and N-terminal two-strand parallel beta-sheets from each monomer. C-PhnF shares strong structural similarity with the chorismate lyase fold, which features a buried active site locked behind two helix-turn-helix loops. The structural comparison of the C-PhnF and UbiC proteins allows us to propose that a similar site in the PhnF structure is adapted for effector binding.
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