1AB8

RAT TYPE II ADENYLYL CYCLASE C2 DOMAIN/FORSKOLIN COMPLEX

Summary for 1AB8

• Entry DOI: 10.2210/pdb1ab8/pdb
• Descriptor: ADENYLYL CYCLASE, FORSKOLIN (3 entities in total)
• Functional Keywords: lyase, adenylyl cyclase, plasmid, complex (transferase-inhibitor)
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Membrane ; Multi-pass membrane protein : P26769
• Total number of polymer chains: 2
• Total formula weight: 49716.56

Authors

Zhang, G.,Hurley, J.H. (deposition date: 1997-02-04, release date: 1997-05-15, Last modification date: 2024-02-07)

Primary citation

Zhang, G.,Liu, Y.,Ruoho, A.E.,Hurley, J.H.
Structure of the adenylyl cyclase catalytic core.
Nature, 386:247-253, 1997

PubMed Abstract: Mammalian adenylyl cyclases contain two conserved regions, C1 and C2, which are responsible for forskolin- and G-protein-stimulated catalysis. The structure of the C2 catalytic region of type II rat adenylyl cyclase has an alpha/beta class fold in a wreath-like dimer, which has a central cleft. Two forskolin molecules bind in hydrophobic pockets at the ends of cleft. The central part of the cleft is lined by charged residues implicated in ATP binding. Forskolin appears to activate adenylyl cyclase by promoting the assembly of the active dimer and by direct interaction within the catalytic cleft. Other adenylyl cyclase regulators act at the dimer interface or on a flexible C-terminal region.

PubMed: 9069282
DOI: 10.1038/386247a0

Experimental method

X-RAY DIFFRACTION (2.2 Å)