1CJU

COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH BETA-L-2',3'-DIDEOXYATP AND MG

Summary for 1CJU

• Entry DOI: 10.2210/pdb1cju/pdb
• Descriptor: ADENYLATE CYCLASE, TYPE V, ADENYLATE CYCLASE, TYPE II, GUANINE NUCLEOTIDE-BINDING PROTEIN G(S), ... (9 entities in total)
• Functional Keywords: complex (lyase-hydrolase), hydrolase, signal transducing protein, cyclase, effector enzyme, lyase-lyase-signaling protein complex, lyase/lyase/signaling protein
• Biological source: Canis lupus (dog); More
• Cellular location: Membrane; Multi-pass membrane protein: P30803 P26769; Cell membrane; Lipid-anchor (By similarity): P04896
• Total number of polymer chains: 3
• Total formula weight: 96402.13

Authors

Tesmer, J.J.G.,Sprang, S.R. (deposition date: 1999-04-16, release date: 1999-08-31, Last modification date: 2023-08-02)

Primary citation

Tesmer, J.J.,Sunahara, R.K.,Johnson, R.A.,Gosselin, G.,Gilman, A.G.,Sprang, S.R.
Two-metal-Ion catalysis in adenylyl cyclase.
Science, 285:756-760, 1999

PubMed Abstract: Adenylyl cyclase (AC) converts adenosine triphosphate (ATP) to cyclic adenosine monophosphate, a ubiquitous second messenger that regulates many cellular functions. Recent structural studies have revealed much about the structure and function of mammalian AC but have not fully defined its active site or catalytic mechanism. Four crystal structures were determined of the catalytic domains of AC in complex with two different ATP analogs and various divalent metal ions. These structures provide a model for the enzyme-substrate complex and conclusively demonstrate that two metal ions bind in the active site. The similarity of the active site of AC to those of DNA polymerases suggests that the enzymes catalyze phosphoryl transfer by the same two-metal-ion mechanism and likely have evolved from a common ancestor.

PubMed: 10427002
DOI: 10.1126/science.285.5428.756

Experimental method

X-RAY DIFFRACTION (2.8 Å)