ArticleScientific reports2016
Structural insights into the Escherichia coli lysine decarboxylases and molecular determinants of interaction with the AAA+ ATPase RavA.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 43 citations in OpenAlex.
- Characterization and Immobilization of a High Activity Lysine Decarboxylase from Serratia Proteamaculans NJ303 for Cadaverine Production.Applied biochemistry and biotechnology · 2026Article
- Amino acids and their metabolites as potential biochemical markers in postmortem vitreous humour.International journal of legal medicine · 2025Article
- Region-based segmental swapping of homologous enzymes for higher cadaverine production.Microbial cell factories · 2025Article
- Dataset from a human-in-the-loop approach to identify functionally important protein residues from literature.Scientific data · 2024Article
- Rationally Engineering pH Adaptation of Acid-Induced Arginine Decarboxylase from Escherichia coli to Alkaline Environments to Efficiently Biosynthesize Putrescine.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Tradeoffs Between Evolved Phage Resistance and Antibiotic Susceptibility in a Highly Drug-Resistant Cystic Fibrosis-DerivedPHAGE (New Rochelle, N.Y.) · 2024Article
- RavA-ViaA antibiotic response is linked to Cpx and Zra2 envelope stress systems inMicrobiology spectrum · 2023Article
- The RavA-ViaA chaperone complex modulates bacterial persistence through its association with the fumarate reductase enzyme.The Journal of biological chemistry · 2023Article
- The AAA+ ATPase RavA and its binding partner ViaA modulate E. coli aminoglycoside sensitivity through interaction with the inner membrane.Nature communications · 2022Article
- Green chemical and biological synthesis of cadaverine: recent development and challenges.RSC advances · 2021Review
- Resolving the Contradictory Functions of Lysine Decarboxylase and Butyrate in Periodontal and Intestinal Diseases.Journal of clinical medicine · 2021Review
- Biochemical Characterization and Structural Insight into Interaction and Conformation Mechanisms ofMolecules (Basel, Switzerland) · 2021Article
- Structural and functional analysis of the Francisella lysine decarboxylase as a key actor in oxidative stress resistance.Scientific reports · 2021Article
- Supramolecular assembly of theProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Comparative Review of the Responses ofGenes · 2020Review
- Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex.Communications biology · 2020Article
- Adaptational changes in physiological and transcriptional responses of Bifidobacterium longum involved in acid stress resistance after successive batch cultures.Microbial cell factories · 2019Article
- Tailoring the properties of (catalytically)-active inclusion bodies.Microbial cell factories · 2019Article
- A Novel Subfamily of Bacterial AAT-Fold Basic Amino Acid Decarboxylases and Functional Characterization of Its First Representative: Pseudomonas aeruginosa LdcA.Genome biology and evolution · 2018Article
- Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production.Scientific reports · 2018Article
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The inducible lysine decarboxylase LdcI is an important enterobacterial acid stress response enzyme whereas LdcC is its close paralogue thought to play mainly a metabolic role. A unique macromolecular cage formed by two decamers of the Escherichia coli LdcI and five hexamers of the AAA+ ATPase RavA was shown to counteract acid stress under starvation. Previously, we proposed a pseudoatomic model of the LdcI-RavA cage based on its cryo-electron microscopy map and crystal structures of an inactive LdcI decamer and a RavA monomer. We now present cryo-electron microscopy 3D reconstructions of the E. coli LdcI and LdcC, and an improved map of the LdcI bound to the LARA domain of RavA, at pH optimal for their enzymatic activity. Comparison with each other and with available structures uncovers differences between LdcI and LdcC explaining why only the acid stress response enzyme is capable of binding RavA. We identify interdomain movements associated with the pH-dependent enzyme activation and with the RavA binding. Multiple sequence alignment coupled to a phylogenetic analysis reveals that certain enterobacteria exert evolutionary pressure on the lysine decarboxylase towards the cage-like assembly with RavA, implying that this complex may have an important function under particular stress conditions.
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