ArticleThe EMBO journal2005
Origin of asymmetry in adenylyl cyclases: structures of Mycobacterium tuberculosis Rv1900c.
Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.
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Who cites it
32 citing papers in PubMed, 1 synthesis or guideline pooled it, 78 citations in OpenAlex.
- The evolutionary conservation of eukaryotic membrane-bound adenylyl cyclase isoforms.Frontiers in pharmacology · 2022Pooled it
- ATP-dependent conformational dynamics in a photoactivated adenylate cyclase revealed by fluorescence spectroscopy and small-angle X-ray scattering.Communications biology · 2024Article
- Mycobacterial STAND adenylyl cyclases: The HTH domain binds DNA to form biocrystallized nucleoids.Biophysical journal · 2021Article
- Rv1288, a Two Domain, Cell Wall Anchored, Nutrient Stress Inducible Carboxyl-Esterase ofFrontiers in cellular and infection microbiology · 2018Article
- Role of the nucleotidyl cyclase helical domain in catalytically active dimer formation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structural Basis for the Strict Substrate Selectivity of the Mycobacterial Hydrolase LipW.Biochemistry · 2016Article
- Article
- Crystal structures of human soluble adenylyl cyclase reveal mechanisms of catalysis and of its activation through bicarbonate.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Mutational analysis gives insight into substrate preferences of a nucleotidyl cyclase from Mycobacterium avium.PloS one · 2014Article
- The role of transcriptional regulation in maintaining the availability of mycobacterial adenylate cyclases.PeerJ · 2014Article
- Expression of a subset of heat stress induced genes of mycobacterium tuberculosis is regulated by 3',5'-cyclic AMP.PloS one · 2014Article
- Characterization of an acid inducible lipase Rv3203 from Mycobacterium tuberculosis H37Rv.Molecular biology reports · 2014Article
- Overexpression of the Rv0805 phosphodiesterase elicits a cAMP-independent transcriptional response.Tuberculosis (Edinburgh, Scotland) · 2013Article
- CRISPR interference: a structural perspective.The Biochemical journal · 2013Review
- Article
- Phosphatidylinositol-4-phosphate 5-kinase isoforms exhibit acyl chain selectivity for both substrate and lipid activator.The Journal of biological chemistry · 2012Article
- Guanylyl cyclases A and B are asymmetric dimers that are allosterically activated by ATP binding to the catalytic domain.Science signaling · 2012Article
- The S-helix determines the signal in a Tsr receptor/adenylyl cyclase reporter.The Journal of biological chemistry · 2012Article
- Structure of the Cmr2 subunit of the CRISPR-Cas RNA silencing complex.Structure (London, England : 1993) · 2012Article
- Crystal structure and regulation mechanisms of the CyaB adenylyl cyclase from the human pathogen Pseudomonas aeruginosa.Journal of molecular biology · 2012Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Rv1900c, a Mycobacterium tuberculosis adenylyl cyclase, is composed of an N-terminal alpha/beta-hydrolase domain and a C-terminal cyclase homology domain. It has an unusual 7% guanylyl cyclase side-activity. A canonical substrate-defining lysine and a catalytic asparagine indispensable for mammalian adenylyl cyclase activity correspond to N342 and H402 in Rv1900c. Mutagenic analysis indicates that these residues are dispensable for activity of Rv1900c. Structures of the cyclase homology domain, solved to 2.4 A both with and without an ATP analog, form isologous, but asymmetric homodimers. The noncanonical N342 and H402 do not interact with the substrate. Subunits of the unliganded open dimer move substantially upon binding substrate, forming a closed dimer similar to the mammalian cyclase heterodimers, in which one interfacial active site is occupied and the quasi-dyad-related active site is occluded. This asymmetry indicates that both active sites cannot simultaneously be catalytically active. Such a mechanism of half-of-sites-reactivity suggests that mammalian heterodimeric adenylyl cyclases may have evolved from gene duplication of a primitive prokaryote-type cyclase, followed by loss of function in one active site.
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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.