ArticleActa crystallographica. Section F, Structural biology and crystallization communications2007
Oligomerization of BenM, a LysR-type transcriptional regulator: structural basis for the aggregation of proteins in this family.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2007. 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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17 citing papers in PubMed, 37 citations in OpenAlex.
- Fundamentals and Exceptions of the LysR-type Transcriptional Regulators.ACS synthetic biology · 2024Review
- Evolving Small-Molecule Biosensors with Improved Performance and Reprogrammed Ligand Preference Using OrthoRep.ACS synthetic biology · 2021Article
- A novel LysR-type regulator negatively affects biosynthesis of the immunosuppressant brasilicardin.Engineering in life sciences · 2021Article
- Evolution-guided engineering of small-molecule biosensors.Nucleic acids research · 2020Article
- DbdR, a New Member of the LysR Family of Transcriptional Regulators, Coordinately Controls Four Promoters in the Thauera aromatica AR-1 3,5-Dihydroxybenzoate Anaerobic Degradation Pathway.Applied and environmental microbiology · 2019Article
- Crystal structure of the ligand-binding domain of a LysR-type transcriptional regulator: transcriptional activation via a rotary switch.Molecular microbiology · 2018Article
- Molecular determinants of Burkholderia pseudomallei BpeEF-OprC efflux pump expression.Microbiology (Reading, England) · 2018Article
- Regulation of the aceI multidrug efflux pump gene in Acinetobacter baumannii.The Journal of antimicrobial chemotherapy · 2018Article
- Functional Mechanism of the Efflux Pumps Transcription Regulators FromFrontiers in molecular biosciences · 2018Review
- Ribavirin suppresses bacterial virulence by targeting LysR-type transcriptional regulators.Scientific reports · 2016Article
- The β-lactamase gene regulator AmpR is a tetramer that recognizes and binds the D-Ala-D-Ala motif of its repressor UDP-N-acetylmuramic acid (MurNAc)-pentapeptide.The Journal of biological chemistry · 2015Article
- Article
- Isolation and characterization of mutant Sinorhizobium meliloti NodD1 proteins with altered responses to luteolin.Journal of bacteriology · 2013Article
- The transcription factor AlsR binds and regulates the promoter of the alsSD operon responsible for acetoin formation in Bacillus subtilis.Journal of bacteriology · 2012Article
- Most mutant OccR proteins that are defective in positive control hold operator DNA in a locked high-angle bend.Journal of bacteriology · 2011Article
- Crystallization and preliminary X-ray analysis of CrgA, a LysR-type transcriptional regulator from pathogenic Neisseria meningitidis MC58.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008Article
- Bradyrhizobium elkanii nod regulon: insights through genomic analysis.Genetics and molecular biologyArticle
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
LysR-type transcriptional regulators comprise the largest family of homologous regulatory DNA-binding proteins in bacteria. A problematic challenge in the crystallization of LysR-type regulators stems from the insolubility and precipitation difficulties encountered with high concentrations of the full-length versions of these proteins. A general oligomerization scheme is proposed for this protein family based on the structures of the effector-binding domain of BenM in two different space groups, P4(3)22 and C222(1). These structures used the same oligomerization scheme of dimer-dimer interactions as another LysR-type regulator, CbnR, the full-length structure of which is available [Muraoka et al. (2003), J. Mol. Biol. 328, 555-566]. Evaluation of packing relationships and surface features suggests that BenM can form infinite oligomeric arrays in crystals through these dimer-dimer interactions. By extrapolation to the liquid phase, such dimer-dimer interactions may contribute to the significant difficulty in crystallizing full-length members of this family. The oligomerization of dimeric units to form biologically important tetramers appears to leave unsatisfied oligomerization sites. Under conditions that favor association, such as neutral pH and concentrations appropriate for crystallization, higher order oligomerization could cause solubility problems with purified proteins. A detailed model by which BenM and other LysR-type transcriptional regulators may form these arrays is proposed.
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