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Medientyp:
E-Artikel
Titel:
Role of the nucleotidyl cyclase helical domain in catalytically active dimer formation
Beteiligte:
Vercellino, Irene;
Rezabkova, Lenka;
Olieric, Vincent;
Polyhach, Yevhen;
Weinert, Tobias;
Kammerer, Richard A.;
Jeschke, Gunnar;
Korkhov, Volodymyr M.
Erschienen:
Proceedings of the National Academy of Sciences, 2017
Erschienen in:Proceedings of the National Academy of Sciences
Sprache:
Englisch
DOI:
10.1073/pnas.1712621114
ISSN:
0027-8424;
1091-6490
Entstehung:
Anmerkungen:
Beschreibung:
<jats:title>Significance</jats:title>
<jats:p>Adenylyl and guanylyl cyclases are at the core of cellular signaling. Although the molecular mechanisms of the reactions catalyzed by these enzymes are well established, their structures and biophysical properties remain only partially characterized. Here, we report the structure of the cytosolic domain of a mycobacterial adenylyl cyclase Cya, an evolutionary ancestor of mammalian membrane adenylyl cyclases. The structure reveals the helical domain, a highly conserved structural element that links the catalytic and transmembrane portions of Cya. We show how helical domains bring together the catalytic domains to form functionally active dimers. Our data suggest that the disease-linked mutations in human nucleotidyl cyclases may disrupt the correct assembly of the helical domain, preventing the formation of an active dimeric enzyme.</jats:p>