Role of the nucleotidyl cyclase helical domain in catalytically active dimer formation

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 114; no. 46; pp. E9821 - E9828
• Main Authors: Vercellino, Irene, Rezabkova, Lenka, Olieric, Vincent, Polyhach, Yevhen, Weinert, Tobias, Kammerer, Richard A., Jeschke, Gunnar, Korkhov, Volodymyr M.
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 14.11.2017
• Series: PNAS Plus
• Subjects: Adenylyl Cyclases - chemistry; Adenylyl Cyclases - genetics; Adenylyl Cyclases - metabolism; Amino Acid Substitution; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Biological Sciences; Catalysis; Catalytic Domain; Conserved Sequence; Crystallography, X-Ray; Cytosol - enzymology; Dimerization; Enzyme Activation; Enzyme Stability; Enzymes; Experiments; Guanylate cyclase; Guanylate Cyclase - chemistry; Guanylate Cyclase - genetics; Humans; Integrals; Machinery and equipment; Models, Molecular; Mutagenesis, Site-Directed; Mutant Proteins - chemistry; Mutant Proteins - genetics; Mutant Proteins - metabolism; Mutation; Mycobacterium avium Complex - enzymology; Mycobacterium avium Complex - genetics; PNAS Plus; Protein Conformation; Protein families; Protein structure; Proteins; Receptors, Cell Surface - chemistry; Receptors, Cell Surface - genetics; Retina; Sequence Alignment; Sequence Analysis, Protein; Signal transduction; Signaling; adenylyl cyclase; dimerization; helical domain; Cya; X-ray structure

Nucleotidyl cyclases, includingmembrane-integral and soluble adenylyl and guanylyl cyclases, are central components in a wide range of signaling pathways. These proteins are architecturally diverse, yet many of them share a conserved feature, a helical region that precedes the catalytic cyclase doma...