ArticlePeerJ2015
Cyclic nucleotide binding and structural changes in the isolated GAF domain of Anabaena adenylyl cyclase, CyaB2.
Article in PeerJ, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
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- Coevolving residues distant from the ligand binding site are involved in GAF domain function.Communications chemistry · 2025Article
- BRET-based biosensors for SARS-CoV-2 oligonucleotide detection.Frontiers in bioengineering and biotechnology · 2024Article
- A potential allosteric inhibitor of SARS-CoV-2 main protease (MFrontiers in molecular biosciences · 2024Article
- Protegrin-2, a potential inhibitor for targeting SARS-CoV-2 main protease MComputational and structural biotechnology journal · 2023Article
- Structure-Based Virtual Screening and Functional Validation of Potential Hit Molecules Targeting the SARS-CoV-2 Main Protease.Biomolecules · 2022Article
- A genetically encoded BRET-based SARS-CoV-2 MCommunications chemistry · 2022Article
- Decreased Interfacial Dynamics Caused by the N501Y Mutation in the SARS-CoV-2 S1 Spike:ACE2 Complex.Frontiers in molecular biosciences · 2022Article
- Intracellular Ionic Strength Sensing Using NanoLuc.International journal of molecular sciences · 2021Article
- Identification and Characterization of c-di-GMP Metabolic Enzymes ofFrontiers in microbiology · 2018Article
- Sustained α-catenin Activation at E-cadherin Junctions in the Absence of Mechanical Force.Biophysical journal · 2016Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
GAF domains are a large family of regulatory domains, and a subset are found associated with enzymes involved in cyclic nucleotide (cNMP) metabolism such as adenylyl cyclases and phosphodiesterases. CyaB2, an adenylyl cyclase from Anabaena, contains two GAF domains in tandem at the N-terminus and an adenylyl cyclase domain at the C-terminus. Cyclic AMP, but not cGMP, binding to the GAF domains of CyaB2 increases the activity of the cyclase domain leading to enhanced synthesis of cAMP. Here we show that the isolated GAFb domain of CyaB2 can bind both cAMP and cGMP, and enhanced specificity for cAMP is observed only when both the GAFa and the GAFb domains are present in tandem (GAFab domain). In silico docking and mutational analysis identified distinct residues important for interaction with either cAMP or cGMP in the GAFb domain. Structural changes associated with ligand binding to the GAF domains could not be detected by bioluminescence resonance energy transfer (BRET) experiments. However, amide hydrogen-deuterium exchange mass spectrometry (HDXMS) experiments provided insights into the structural basis for cAMP-induced allosteric regulation of the GAF domains, and differences in the changes induced by cAMP and cGMP binding to the GAF domain. Thus, our findings could allow the development of molecules that modulate the allosteric regulation by GAF domains present in pharmacologically relevant proteins.
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