ArticleBMC structural biology2008
The crystal structure of the catalytic domain of a eukaryotic guanylate cyclase.
Article in BMC structural biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 91 citations in OpenAlex.
- Origins and Molecular Features of a Chimeric Type-P4A ATPase-Guanylate Cyclase from Stramenopiles and Alveolates.International journal of molecular sciences · 2026Article
- Control of cell division by anbioRxiv : the preprint server for biology · 2026Article
- A patatin-like phospholipase mediates Rickettsia parkeri escape from host membranes.Nature communications · 2022Article
- Structural Perspectives on the Mechanism of Soluble Guanylate Cyclase Activation.International journal of molecular sciences · 2021Review
- Chemosensory signal transduction in Caenorhabditis elegans.Genetics · 2021Review
- Identification of Partner Proteins of the AlgaeFrontiers in plant science · 2021Article
- Molecular basis for GTP recognition by light-activated guanylate cyclase RhGC.The FEBS journal · 2020Article
- Mutational landscape of receptor guanylyl cyclase C: Functional analysis and disease-related mutations.IUBMB life · 2020Review
- Crystal structure of MOA in complex with a peptide fragment: A protease caughtCurrent research in structural biology · 2020Article
- Evasion of autophagy mediated by Rickettsia surface protein OmpB is critical for virulence.Nature microbiology · 2019Article
- Instability in a coiled-coil signaling helix is conserved for signal transduction in soluble guanylyl cyclase.Protein science : a publication of the Protein Society · 2019Article
- Article
- Associated Bacteria Affect Sexual Reproduction by Altering Gene Expression and Metabolic Processes in a Biofilm Inhabiting Diatom.Frontiers in microbiology · 2019Article
- COMolecular and cellular biochemistry · 2018Article
- Physiological activation and deactivation of soluble guanylate cyclase.Nitric oxide : biology and chemistry · 2018Review
- Structure/function of the soluble guanylyl cyclase catalytic domain.Nitric oxide : biology and chemistry · 2018Review
- Redox regulation of soluble guanylyl cyclase.Nitric oxide : biology and chemistry · 2018Review
- Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain.Nature communications · 2018Article
- Molecular Details of Retinal Guanylyl Cyclase 1/GCAP-2 Interaction.Frontiers in molecular neuroscience · 2018Article
- Structure and monomer/dimer equilibrium for the guanylyl cyclase domain of the optogenetics protein RhoGC.The Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundSoluble guanylate cyclases generate cyclic GMP when bound to nitric oxide, thereby linking nitric oxide levels to the control of processes such as vascular homeostasis and neurotransmission. The guanylate cyclase catalytic module, for which no structure has been determined at present, is a class III nucleotide cyclase domain that is also found in mammalian membrane-bound guanylate and adenylate cyclases.
resultsWe have determined the crystal structure of the catalytic domain of a soluble guanylate cyclase from the green algae Chlamydomonas reinhardtii at 2.55 A resolution, and show that it is a dimeric molecule.
conclusionComparison of the structure of the guanylate cyclase domain with the known structures of adenylate cyclases confirms the close similarity in architecture between these two enzymes, as expected from their sequence similarity. The comparison also suggests that the crystallized guanylate cyclase is in an inactive conformation, and the structure provides indications as to how activation might occur. We demonstrate that the two active sites in the dimer exhibit positive cooperativity, with a Hill coefficient of approximately 1.5. Positive cooperativity has also been observed in the homodimeric mammalian membrane-bound guanylate cyclases. The structure described here provides a reliable model for functional analysis of mammalian guanylate cyclases, which are closely related in sequence.
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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.