PDBsum entry 6r3q

Membrane protein

PDB id: 6r3q

Contents

Protein chains

841 a.a.

341 a.a.

Ligands

GSP

Metals

_MG

PDB id:

6r3q

Name:

Membrane protein

Title:

The structure of a membrane adenylyl cyclase bound to an activated stimulatory g protein

Structure:

Adenylate cyclase 9. Chain: a. Synonym: adenylyl cyclase family member (acy-1)-like. Engineered: yes. Guanine nucleotide-binding protein g(s) subunit alpha isoforms short. Chain: b. Synonym: adenylate cyclase-stimulating g alpha protein. Engineered: yes

Source:

Bos taurus. Cattle. Organism_taxid: 9913. Gene: adcy9, bos_22626. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293f. Gene: gnas, gnas1. Expressed in: trichoplusia ni.

Authors:

V.M.Korkhov,C.Qi

Key ref:

C.Qi et al. (2019). The structure of a membrane adenylyl cyclase bound to an activated stimulatory G protein. Science, 364, 389-394. PubMed id: 31023924 DOI: 10.1126/science.aav0778

Date:

20-Mar-19 Release date: 08-May-19

Protein chain

E1BM79  (E1BM79_BOVIN) -  adenylate cyclase from Bos taurus

Seq: 1354 a.a.

Struc: 841 a.a.

Protein chain

P04896  (GNAS2_BOVIN) -  Guanine nucleotide-binding protein G(s) subunit alpha isoforms short from Bos taurus

Seq: 394 a.a.

Struc: 341 a.a.

Enzyme reactions

• Enzyme class 1: Chain A: E.C.4.6.1.1 - adenylate cyclase.
• Reaction: ATP = 3',5'-cyclic AMP + diphosphate

ATP (Bound ligand (Het Group name = GSP) matches with 90.91% similarity) = 3',5'-cyclic AMP + diphosphate

• Cofactor: Pyridoxal 5'-phosphate
• Enzyme class 2: Chain B: E.C.?

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1126/science.aav0778

Science 364:389-394 (2019)

PubMed id: 31023924

The structure of a membrane adenylyl cyclase bound to an activated stimulatory G protein.

C.Qi, S.Sorrentino, O.Medalia, V.M.Korkhov.

ABSTRACT

Membrane-integral adenylyl cyclases (ACs) are key enzymes in mammalian heterotrimeric GTP-binding protein (G protein)-dependent signal transduction, which is important in many cellular processes. Signals received by the G protein-coupled receptors are conveyed to ACs through G proteins to modulate the levels of cellular cyclic adenosine monophosphate (cAMP). Here, we describe the cryo-electron microscopy structure of the bovine membrane AC9 bound to an activated G protein αs subunit at 3.4-angstrom resolution. The structure reveals the organization of the membrane domain and helical domain that spans between the membrane and catalytic domains of AC9. The carboxyl-terminal extension of the catalytic domain occludes both the catalytic and the allosteric sites of AC9, inducing a conformation distinct from the substrate- and activator-bound state, suggesting a regulatory role in cAMP production.