[English] 日本語
Yorodumi- EMDB-4721: Structure of a truncated adenylyl cyclase bound to MANT-GTP, fors... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-4721 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Structure of a truncated adenylyl cyclase bound to MANT-GTP, forskolin and an activated stimulatory Galphas protein | |||||||||
Map data | Truncated AC9 (AC9-1250) bound to MANT-GTP, forskolin and GalphaS | |||||||||
Sample |
| |||||||||
Function / homology | Function and homology information Adenylate cyclase activating pathway / Adenylate cyclase inhibitory pathway / sensory perception of chemical stimulus / PKA activation / adenylate cyclase / mu-type opioid receptor binding / Hedgehog 'off' state / corticotropin-releasing hormone receptor 1 binding / cAMP biosynthetic process / adenylate cyclase activity ...Adenylate cyclase activating pathway / Adenylate cyclase inhibitory pathway / sensory perception of chemical stimulus / PKA activation / adenylate cyclase / mu-type opioid receptor binding / Hedgehog 'off' state / corticotropin-releasing hormone receptor 1 binding / cAMP biosynthetic process / adenylate cyclase activity / G alpha (z) signalling events / beta-2 adrenergic receptor binding / D1 dopamine receptor binding / positive regulation of cAMP-mediated signaling / adenylate cyclase-activating adrenergic receptor signaling pathway / ionotropic glutamate receptor binding / insulin-like growth factor receptor binding / adenylate cyclase activator activity / G-protein beta/gamma-subunit complex binding / adenylate cyclase-activating G protein-coupled receptor signaling pathway / positive regulation of GTPase activity / adenylate cyclase-activating dopamine receptor signaling pathway / heterotrimeric G-protein complex / in utero embryonic development / intracellular signal transduction / GTPase activity / GTP binding / metal ion binding / plasma membrane / cytosol Similarity search - Function | |||||||||
Biological species | Bos taurus (cattle) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.2 Å | |||||||||
Authors | Qi C / Sorrentino S / Medalia O / Korkhov VM | |||||||||
Funding support | Switzerland, 1 items
| |||||||||
Citation | Journal: Science / Year: 2019 Title: The structure of a membrane adenylyl cyclase bound to an activated stimulatory G protein. Authors: Chao Qi / Simona Sorrentino / Ohad Medalia / Volodymyr 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. ...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. #1: Journal: To Be Published Title: The structure of a membrane adenylyl cyclase bound to an activated stimulatory G protein Authors: Qi C / Sorrentino S / Medalia O / Korkhov VM | |||||||||
History |
|
-Structure visualization
Movie |
Movie viewer |
---|---|
Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_4721.map.gz | 226.7 MB | EMDB map data format | |
---|---|---|---|---|
Header (meta data) | emd-4721-v30.xml emd-4721.xml | 19 KB 19 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_4721_fsc.xml | 6.8 KB | Display | FSC data file |
Images | emd_4721.png | 67.4 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-4721 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-4721 | HTTPS FTP |
-Related structure data
Related structure data | 6r4oMC 4719C 4722C 4723C 4724C 4725C 4726C 6r3qC 6r4pC M: atomic model generated by this map C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
---|---|
Related items in Molecule of the Month |
-Map
File | Download / File: emd_4721.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Truncated AC9 (AC9-1250) bound to MANT-GTP, forskolin and GalphaS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.8544 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
|
-Supplemental data
-Sample components
+Entire : Adenylyl cyclase AC9 (truncation, residues 1-1250) bound to MANT-...
+Supramolecule #1: Adenylyl cyclase AC9 (truncation, residues 1-1250) bound to MANT-...
+Supramolecule #2: Adenylyl cyclase AC9
+Supramolecule #3: GalphaS protein
+Macromolecule #1: Adenylate cyclase 9
+Macromolecule #2: Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
+Macromolecule #3: 3'-O-(N-METHYLANTHRANILOYL)-GUANOSINE-5'-TRIPHOSPHATE
+Macromolecule #4: FORSKOLIN
+Macromolecule #5: MANGANESE (II) ION
+Macromolecule #6: 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE
+Macromolecule #7: MAGNESIUM ION
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
---|---|
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 278 K / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 2 / Number real images: 10758 / Average electron dose: 60.0 e/Å2 Details: Two datasets were merged using two different microscopes, using pixel size of 0.831 A/pix (4453 micrographs; 60 e-/A2) and 0.8544 A/pix (6305 micrographs; 45 e-/A2). Final dataset was scaled to 0.8544 A/pix. |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: AB INITIO MODEL / Overall B value: 110.92 / Target criteria: Cross-correlation coefficient |
---|---|
Output model | PDB-6r4o: |