Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain

• Published in: Nature communications Vol. 9; no. 1; pp. 2046 - 15
• Main Authors: Scheib, Ulrike, Broser, Matthias, Constantin, Oana M., Yang, Shang, Gao, Shiqiang, Mukherjee, Shatanik, Stehfest, Katja, Nagel, Georg, Gee, Christine E., Hegemann, Peter
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 24.05.2018; Nature Publishing Group; Nature Portfolio
• Subjects: 631/378/340; 631/45/535/1266; 631/45/607; 631/57/2272; 82/16; 82/29; 82/80; 82/83; 9/74; Adenylyl Cyclases - chemistry; Adenylyl Cyclases - genetics; Adenylyl Cyclases - metabolism; Animals; Binding Sites; Blastocladiomycota - chemistry; Blastocladiomycota - enzymology; Blastocladiomycota - genetics; Crystal structure; Crystallization; Cyclic AMP; Cyclic AMP - chemistry; Cyclic AMP - metabolism; Cyclic GMP; Cyclic GMP - chemistry; Cyclic GMP - metabolism; Cyclic nucleotides; Fungal Proteins - chemistry; Fungal Proteins - metabolism; Guanylate cyclase; Guanylate Cyclase - chemistry; Guanylate Cyclase - genetics; Guanylate Cyclase - metabolism; Humanities and Social Sciences; Models, Molecular; multidisciplinary; Mutation; Nucleotides; Protein Binding; Protein Domains; Rats; Rhodopsin; Rhodopsin - chemistry; Rhodopsin - metabolism; Science; Science (multidisciplinary); Second messengers

The cyclic nucleotides cAMP and cGMP are important second messengers that orchestrate fundamental cellular responses. Here, we present the characterization of the rhodopsin-guanylyl cyclase from Catenaria anguillulae (CaRhGC), which produces cGMP in response to green light with a light to dark activ...