ArticleJournal of molecular biology2007
Structure of the Escherichia coli leucine-responsive regulatory protein Lrp reveals a novel octameric assembly.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
53 citing papers in PubMed, 102 citations in OpenAlex.
- Nucleoid-associated proteins: molecular mechanisms in microbial adaptation.World journal of microbiology & biotechnology · 2025Review
- A leucine responsive small RNA AbcR200 regulates expression of the lactate utilization (lut) operon in Acinetobacter baumannii DS002.The Journal of biological chemistry · 2025Article
- Synthesis and Degradation of the Phytohormone Indole-3-Acetic Acid by the Versatile BacteriumPlants (Basel, Switzerland) · 2024Article
- Improving the production of carbamoyltobramycin by an industrial Streptoalloteichus tenebrarius through metabolic engineering.Applied microbiology and biotechnology · 2024Article
- Molecular mechanisms of regulation by a β-alanine-responsive Lrp-type transcription factor from Acidianus hospitalis.MicrobiologyOpen · 2023Article
- The type-VI secretion system of the beneficial symbiontMicrobiology (Reading, England) · 2023Review
- Pneumococcal capsule expression is controlled through a conserved, distal cis-regulatory element during infection.PLoS pathogens · 2023Article
- The Lrp/AsnC-Type Regulator PA2577 Controls the EamA-like Transporter GeneInternational journal of molecular sciences · 2021Article
- Leucine-Responsive Regulatory Protein in Acetic Acid Bacteria Is Stable and Functions at a Wide Range of Intracellular pH Levels.Journal of bacteriology · 2021Article
- The leucine-responsive regulatory proteins/feast-famine regulatory proteins: an ancient and complex class of transcriptional regulators in bacteria and archaea.Critical reviews in biochemistry and molecular biology · 2021Review
- A Thermosensitive, Phase-Variable Epigenetic Switch:Microbiology and molecular biology reviews : MMBR · 2020Review
- Clusters of bacterial RNA polymerase are biomolecular condensates that assemble through liquid-liquid phase separation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Evolution of Regulated Transcription.Cells · 2020Review
- Chromosomal Organization and Regulation of Genetic Function inEcoSal Plus · 2020Article
- CopR, a Global Regulator of Transcription to Maintain Copper Homeostasis inFrontiers in microbiology · 2020Article
- Regulation of γ-Aminobutyrate (GABA) Utilization inFrontiers in microbiology · 2020Article
- Engineering of leucine-responsive regulatory protein improves spiramycin and bitespiramycin biosynthesis.Microbial cell factories · 2019Article
- Alanine dehydrogenases in mycobacteria.Journal of microbiology (Seoul, Korea) · 2019Review
- Article
- Competitive Repression of theFrontiers in microbiology · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The structure of Escherichia coli leucine-responsive regulatory protein (Lrp) co-crystallized with a short duplex oligodeoxynucleotide reveals a novel quaternary assembly in which the protein octamer forms an open, linear array of four dimers. In contrast, structures of the Lrp homologs LrpA, LrpC and AsnC crystallized in the absence of DNA show that these proteins instead form highly symmetrical octamers in which the four dimers form a closed ring. Although the DNA is disordered within the Lrp crystal, comparative analyses suggest that the observed differences in quaternary state may arise from DNA interactions during crystallization. Interconversion of these conformations, possibly in response to DNA or leucine binding, provides an underlying mechanism to alter the relative spatial orientation of the DNA-binding domains. Breaking of the closed octamer symmetry may be a common essential step in the formation of active DNA complexes by all members of the Lrp/AsnC family of transcriptional regulatory proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.