ArticleProceedings of the National Academy of Sciences of the United States of America2010
Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 48 citations in OpenAlex.
- Structural modeling and biochemical characterization of MSMEG_0748, a MoxR ATPase fromComputational and structural biotechnology journal · 2025Article
- Translation Fidelity and Respiration Deficits in CLPP-Deficient Tissues: Mechanistic Insights from Mitochondrial Complexome Profiling.International journal of molecular sciences · 2023Article
- The RavA-ViaA chaperone complex modulates bacterial persistence through its association with the fumarate reductase enzyme.The Journal of biological chemistry · 2023Article
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- An Estuarine Cyanophage S-CREM1 Encodes Three Distinct Antitoxin Genes and a Large Number of Non-Coding RNA Genes.Viruses · 2023Article
- The AAA+ ATPase RavA and its binding partner ViaA modulate E. coli aminoglycoside sensitivity through interaction with the inner membrane.Nature communications · 2022Article
- Structural and biochemical characterisation of the Providencia stuartii arginine decarboxylase shows distinct polymerisation and regulation.Communications biology · 2022Article
- Green chemical and biological synthesis of cadaverine: recent development and challenges.RSC advances · 2021Review
- 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
- Article
- Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex.Communications biology · 2020Article
- Insights into the mechanism and regulation of the CbbQO-type Rubisco activase, a MoxR AAA+ ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- 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
- The Diverse AAA+ Machines that Repair Inhibited Rubisco Active Sites.Frontiers in molecular biosciences · 2017Review
- Transcriptomes of the Extremely Thermoacidophilic Archaeon Metallosphaera sedula Exposed to Metal "Shock" Reveal Generic and Specific Metal Responses.Applied and environmental microbiology · 2016Article
- Structural insights into the Escherichia coli lysine decarboxylases and molecular determinants of interaction with the AAA+ ATPase RavA.Scientific reports · 2016Article
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- Identification and characterization of multiple rubisco activases in chemoautotrophic bacteria.Nature communications · 2015Article
- Article
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
Abstract
The MoxR family of AAA+ ATPases is widespread throughout bacteria and archaea but remains poorly characterized. We recently found that the Escherichia coli MoxR protein, RavA (Regulatory ATPase variant A), tightly interacts with the inducible lysine decarboxylase, LdcI/CadA, to form a unique cage-like structure. Here, we present the X-ray structure of RavA and show that the αβα and all-α subdomains in the RavA AAA+ module are arranged as in magnesium chelatases rather than as in classical AAA+ proteins. RavA structure also contains a discontinuous triple-helical domain as well as a β-barrel-like domain forming a unique fold, which we termed the LARA domain. The LARA domain was found to mediate the interaction between RavA and LdcI. The RavA structure provides insights into how five RavA hexamers interact with two LdcI decamers to form the RavA-LdcI cage-like structure.
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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.