ArticleThe Journal of biological chemistry2016
Structural and Biochemical Insight into the Mechanism of Rv2837c from Mycobacterium tuberculosis as a c-di-NMP Phosphodiesterase.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 66 citations in OpenAlex.
- Molecular basis of SAM-AMP synthesis and degradation in the type III-B CRISPR-Cas system.Nature chemical biology · 2026Article
- Structural and biochemical insights into the inhibition ofRSC chemical biology · 2026Article
- Orn-mediated c-di-GMP regulates the CRISPR-Cas system to confer stress response in Mycobacterium tuberculosis.Nucleic acids research · 2026Article
- The c-di-AMP binding protein NadD from Mesomycoplasma ovipneumoniae functions as a phosphodiesterase that inhibits host inflammatory responses.Veterinary research · 2026Article
- Functional analyses of bacterial NanoRNase B proteins reveals defining features of this enzyme family.Nucleic acids research · 2025Article
- Discovery of natural CdnP inhibitors through structure-based virtual screening and molecular dynamics simulations.Microbiology spectrum · 2025Article
- Review
- An HPLC-based Assay to Study the Activity of Cyclic Diadenosine Monophosphate (C-di-AMP) Synthase DisA fromBio-protocol · 2024Article
- Synthesis and degradation of the cyclic dinucleotide messenger c-di-AMP in the hyperthermophilic archaeon Pyrococcus yayanosii.Protein science : a publication of the Protein Society · 2023Article
- Bacillus subtilis NrnB is expressed during sporulation and acts as a unique 3'-5' exonuclease.Nucleic acids research · 2023Article
- Article
- Nano-RNases: oligo- or dinucleases?FEMS microbiology reviews · 2022Review
- Expression of a novel mycobacterial phosphodiesterase successfully lowers cAMP levels resulting in reduced tolerance to cell wall-targeting antimicrobials.The Journal of biological chemistry · 2022Article
- NrnA Is a Linear Dinucleotide Phosphodiesterase with Limited Function in Cyclic Dinucleotide Metabolism in Listeria monocytogenes.Journal of bacteriology · 2022Article
- Cyclic-di-AMP Phosphodiesterase Elicits Protective Immune Responses AgainstFrontiers in cellular and infection microbiology · 2022Article
- c-di-AMP Accumulation Regulates Growth, Metabolism, and Immunogenicity ofFrontiers in microbiology · 2022Article
- Structure and Function of Piezophilic HyperthermophilicInternational journal of molecular sciences · 2021Article
- A Luminescence-Based Coupled Enzyme Assay Enables High-Throughput Quantification of the Bacterial Second Messenger 3'3'-Cyclic-Di-AMP.Chembiochem : a European journal of chemical biology · 2021Article
- A decade of research on the second messenger c-di-AMP.FEMS microbiology reviews · 2020Review
- Rapidly Correcting Frameshift Mutations in the Mycobacterium tuberculosisAntimicrobial agents and chemotherapy · 2020Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The intracellular infections of Mycobacterium tuberculosis, which is the causative agent of tuberculosis, are regulated by many cyclic dinucleotide signaling. Rv2837c from M. tuberculosis is a soluble, stand-alone DHH-DHHA1 domain phosphodiesterase that down-regulates c-di-AMP through catalytic degradation and plays an important role in M. tuberculosis infections. Here, we report the crystal structure of Rv2837c (2.0 Å), and its complex with hydrolysis intermediate 5'-pApA (2.35 Å). Our structures indicate that both DHH and DHHA1 domains are essential for c-di-AMP degradation. Further structural analysis shows that Rv2837c does not distinguish adenine from guanine, which explains why Rv2837c hydrolyzes all linear dinucleotides with almost the same efficiency. We observed that Rv2837c degraded other c-di-NMPs at a lower rate than it did on c-di-AMP. Nevertheless, our data also showed that Rv2837c significantly decreases concentrations of both c-di-AMP and c-di-GMP in vivo. Our results suggest that beside its major role in c-di-AMP degradation Rv2837c could also regulate c-di-GMP signaling pathways in bacterial cell.
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