Bifunctional structure of two adenylyl cyclases from the myxobacterium Stigmatella aurantiaca

Coudart-Cavalli, M.P.; Sismeiro, Odile; Danchin, Antoine

doi:10.1016/s0300-9084(97)86934-9

Cited by 20 publications

(14 citation statements)

References 34 publications

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“…Typically, ACs are highly specific for ATP with no detectable activity with GTP (Coudart-Cavalli et al 1997;Guo et al 2001;Kasahara et al 2001;Linder et al 2002Linder et al , 2004Shenoy et al 2005;Sunahara et al 1998;Weber et al 2004), although Cya1, an AC from Rhizobium meliloti has detectable GC activity (Beuve et al 1993). In comparison, various GCs have been shown to have significant AC activity also (Beuve 1999;Linder et al 1999Linder et al , 2000Sunahara et al 1998;Tucker et al 1998).…”

Section: Base Recognition By Chd Active Sitesmentioning

confidence: 99%

Structures, mechanism, regulation and evolution of class III nucleotidyl cyclases

Sinha¹,

Sprang²

2006

Reviews of Physiology Biochemistry and Pharmacology

103

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Cyclic 3 ,5 -guanylyl and adenylyl nucleotides function as second messengers in eukaryotic signal transduction pathways and as sensory transducers in prokaryotes. The nucleotidyl cyclases (NCs) that catalyze the synthesis of these molecules comprise several evolutionarily distinct groups, of which class III is the largest. The domain structures of prokaryotic and eukaryotic class III NCs are diverse, including a variety of regulatory and transmembrane modules. Yet all members of this family contain one or two catalytic domains, characterized by an evolutionarily ancient topological motif (βααββαβ) that is preserved in several other enzymes that catalyze the nucleophilic attack of a 3 -hydroxyl upon a 5 nucleotide phosphate. Two dyad-related catalytic domains compose one catalytic unit, with the catalytic sites formed at the domain interface. The catalytic domains of mononucleotidyl cyclases (MNCs) and diguanylate cyclases (DGCs) are called cyclase homology domains (CHDs) and GGDEF domains, respectively. Prokaryotic NCs usually contain only one catalytic domain and are catalytically active as intermolecular homodimers. The different modes of dimerization in class III NCs probably evolved concurrently with their mode of binding substrate. The catalytic mechanism of GGDEF domain homodimers is not completely understood, but they are expected to have a single active site with each subunit contributing equivalent determinants to bind one GTP molecule or half a c-diGMP molecule. CHD dimers have two potential dyad-related active sites, with both CHDs contributing determinants to each site. Homodimeric class III MNCs have two equivalent catalytic sites, although such enzymes may show half-of-sites reactivity. Eukaryotic class III MNCs often contain two divergent CHDs, with only one catalytically competent site. All CHDs appear to use a common catalytic mechanism, which requires the participation of two magnesium Pharmacol (2006) or manganese ions for binding polyphosphate groups and nucleophile activation. In contrast, mechanisms for purine recognition and specificity are more diverse. Class III NCs are subject to regulation by small molecule effectors, endogenous domains, or exogenous protein partners. Many of these regulators act by altering the interface of the catalytic domains and therefore the integrity of the catalytic site(s). This review focuses on both conserved and divergent mechanisms of class III NC function and regulation.

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Section: Base Recognition By Chd Active Sitesmentioning

confidence: 99%

Structures, mechanism, regulation and evolution of class III nucleotidyl cyclases

Sinha¹,

Sprang²

2006

Reviews of Physiology Biochemistry and Pharmacology

103

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“…Stigmatella aurantiaca B17R20 is a myxobacterium from which two ACs have been identified (20). We expressed amino acids 160 to 353 of cyaB as a recombinant protein (cyaB ) that contained a threonine residue (T293) at the position corresponding to cyaB1 T721 ( Figure 1A).…”

Section: Ac Assaymentioning

confidence: 99%

A Defined Subset of Adenylyl Cyclases Is Regulated by Bicarbonate Ion

Cann

Hammer²,

Zhou

et al. 2003

Journal of Biological Chemistry

100

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“…Prokaryotic receptor-type nucleotide cyclases have been identified previously only in cyanobacteria (Katayama and Ohmori 1997), and putative prokaryotic integral membrane cyclases have been reported in Stigmatella aurantiaca (Coudart-Cavalli et al 1997) and M. tuberculosis (Tang and Hurley 1998), although how the activity of these enzymes is regulated is unknown.…”

Section: Cnmp-binding Proteins and Cyclases Classificationmentioning

confidence: 99%

Functional Classification of cNMP-binding Proteins and Nucleotide Cyclases with Implications for Novel Regulatory Pathways in Mycobacterium tuberculosis

McCue¹,

McDonough²,

Lawrence³

2000

Genome Res.

133

162

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We have analyzed the cyclic nucleotide (cNMP)-binding protein and nucleotide cyclase superfamilies using Bayesian computational methods of protein family identification and classification. In addition to the known cNMP-binding proteins (cNMP-dependent kinases, cNMP-gated channels, cAMP-guanine nucleotide exchange factors, and bacterial cAMP-dependent transcription factors), new functional groups of cNMP-binding proteins were identified, including putative ABC-transporter subunits, translocases, and esterases. Classification of the nucleotide cyclases revealed subtle differences in sequence conservation of the active site that distinguish the five classes of cyclases: the multicellular eukaryotic adenylyl cyclases, the eukaryotic receptor-type guanylyl cyclases, the eukaryotic soluble guanylyl cyclases, the unicellular eukaryotic and prokaryotic adenylyl cyclases, and the putative prokaryotic guanylyl cyclases. Phylogenetic distribution of the cNMP-binding proteins and cyclases was analyzed, with particular attention to the 22 complete archaeal and eubacterial genome sequences. Mycobacterium tuberculosis H37Rv and Synechocystis PCC6803 were each found to encode several more putative cNMP-binding proteins than other prokaryotes; many of these proteins are of unknown function. M. tuberculosis also encodes several more putative nucleotide cyclases than other prokaryotic species.Signal transduction pathways control many critical cellular processes, including chemotaxis, differentiation, proliferation, and apoptosis. For example, signal transduction pathways are necessary for bacterial pathogens to sense and respond to host environments, cellular differentiation during embryogenesis, conductance of nerve impulses, and cell cycle control. Disruption of these pathways can result in neoplasia, arteriosclerosis, neurological and developmental abnormalities, and cell death. The most common mechanisms of signal transduction include the phosphorylation or dephosphorylation of effector proteins by kinases and phosphatases, respectively, and the production of second messengers. Cyclic nucleotides were first recognized as second messengers 40 years ago. Such diverse molecules as (p)ppGpp, Ca 2+ , inositol triphosphate, and diacylglycerol have also been recognized as second messengers since then.The cyclic nucleotides adenosine 3Ј,5Ј-cyclic monophosphate (cAMP) and guanosine 3Ј,5Ј-cyclic monophosphate (cGMP) are key universal second messengers, mediating cellular functions in organisms as phylogenetically diverse as Escherichia coli and Homo sapiens. Intracellular concentrations of cyclic nucleotides (cNMPs) are controlled by regulation of their relative rates of synthesis, excretion, and degradation (Botsford and Harman 1992;). The nucleotide cyclases (adenylyl and guanylyl cyclase), the cNMP phosphodiesterases, and the cyclic nucleotide effector proteins (cNMP-binding proteins) have been particularly intense areas of signal transduction research, providing detailed studies of these proteins (for reviews, see Kolb et

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Bifunctional structure of two adenylyl cyclases from the myxobacterium Stigmatella aurantiaca

Cited by 20 publications

References 34 publications

Structures, mechanism, regulation and evolution of class III nucleotidyl cyclases

Structures, mechanism, regulation and evolution of class III nucleotidyl cyclases

A Defined Subset of Adenylyl Cyclases Is Regulated by Bicarbonate Ion

Functional Classification of cNMP-binding Proteins and Nucleotide Cyclases with Implications for Novel Regulatory Pathways in Mycobacterium tuberculosis

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