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- EMDB-63823: Cryo-EM structure of human AC9-Gs complex (soluble domain) -

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Basic information

Entry
Database: EMDB / ID: EMD-63823
TitleCryo-EM structure of human AC9-Gs complex (soluble domain)
Map datamain map
Sample
  • Complex: human AC9 in complex with GalphaS
    • Protein or peptide: Adenylate cyclase type 9,Protein M2-1
    • Protein or peptide: Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
  • Ligand: 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE
  • Ligand: MAGNESIUM ION
Keywordsenzyme / MEMBRANE PROTEIN
Function / homology
Function and homology information


Adenylate cyclase activating pathway / regulation of viral transcription / adenylate cyclase / cAMP biosynthetic process / adenylate cyclase activity / PKA activation / viral transcription / PKA activation in glucagon signalling / developmental growth / hair follicle placode formation ...Adenylate cyclase activating pathway / regulation of viral transcription / adenylate cyclase / cAMP biosynthetic process / adenylate cyclase activity / PKA activation / viral transcription / PKA activation in glucagon signalling / developmental growth / hair follicle placode formation / D1 dopamine receptor binding / intracellular transport / vascular endothelial cell response to laminar fluid shear stress / renal water homeostasis / activation of adenylate cyclase activity / Hedgehog 'off' state / Adenylate cyclase inhibitory pathway / adenylate cyclase-activating adrenergic receptor signaling pathway / cellular response to glucagon stimulus / regulation of insulin secretion / FCGR3A-mediated IL10 synthesis / bioluminescence / adenylate cyclase activator activity / trans-Golgi network membrane / generation of precursor metabolites and energy / transcription antitermination / negative regulation of inflammatory response to antigenic stimulus / bone development / virion component / platelet aggregation / G-protein beta/gamma-subunit complex binding / cognition / adenylate cyclase-activating G protein-coupled receptor signaling pathway / Prostacyclin signalling through prostacyclin receptor / Glucagon signaling in metabolic regulation / Glucagon-type ligand receptors / Vasopressin regulates renal water homeostasis via Aquaporins / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / G alpha (z) signalling events / cellular response to catecholamine stimulus / ADORA2B mediated anti-inflammatory cytokines production / sensory perception of smell / adenylate cyclase-activating dopamine receptor signaling pathway / GPER1 signaling / cellular response to prostaglandin E stimulus / heterotrimeric G-protein complex / positive regulation of cold-induced thermogenesis / G protein activity / High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells / G alpha (i) signalling events / G alpha (s) signalling events / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / in utero embryonic development / host cell cytoplasm / intracellular signal transduction / cilium / ciliary basal body / G protein-coupled receptor signaling pathway / axon / GTPase activity / dendrite / GTP binding / host cell nucleus / structural molecule activity / signal transduction / extracellular exosome / zinc ion binding / ATP binding / metal ion binding / membrane / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Pneumovirus matrix 2-1 / Pneumovirus matrix protein 2 (M2) / Adenylyl cyclase class-4/guanylyl cyclase, conserved site / Guanylate cyclase signature. / Adenylyl- / guanylyl cyclase, catalytic domain / Adenylate and Guanylate cyclase catalytic domain / Adenylyl cyclase class-3/4/guanylyl cyclase / Guanylate cyclase domain profile. / Zinc finger, CCCH-type / Zinc finger C3H1-type profile. ...Pneumovirus matrix 2-1 / Pneumovirus matrix protein 2 (M2) / Adenylyl cyclase class-4/guanylyl cyclase, conserved site / Guanylate cyclase signature. / Adenylyl- / guanylyl cyclase, catalytic domain / Adenylate and Guanylate cyclase catalytic domain / Adenylyl cyclase class-3/4/guanylyl cyclase / Guanylate cyclase domain profile. / Zinc finger, CCCH-type / Zinc finger C3H1-type profile. / Nucleotide cyclase / G-protein alpha subunit, group S / Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / Guanine nucleotide binding protein (G-protein), alpha subunit / G protein alpha subunit, helical insertion / G-protein alpha subunit / G-alpha domain profile. / G protein alpha subunit / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Protein M2-1 / Adenylate cyclase type 9 / Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Similarity search - Component
Biological speciesHomo sapiens (human) / Human respiratory syncytial virus
Methodsingle particle reconstruction / cryo EM / Resolution: 2.65 Å
AuthorsSuzuki S / Nomura R / Suzuki H / Nishikawa K / Fujiyoshi Y
Funding support Japan, 2 items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS)20H00451 Japan
Japan Society for the Promotion of Science (JSPS)20K17245 Japan
CitationJournal: To Be Published
Title: Activation mechanism of human adenylyl cyclase 9 observed by cryo-electron microscopy
Authors: Nomura S / Suzuki S / Nishikawa K / Suzuki H / Fujiyoshi Y
History
DepositionMar 18, 2025-
Header (metadata) releaseJun 11, 2025-
Map releaseJun 11, 2025-
UpdateJun 11, 2025-
Current statusJun 11, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_63823.png

Downloads & links

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Map

FileDownload / File: emd_63823.map.gz / Format: CCP4 / Size: 95 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationmain map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.79 Å/pix.
x 292 pix.
= 230.68 Å		0.79 Å/pix.
x 292 pix.
= 230.68 Å		0.79 Å/pix.
x 292 pix.
= 230.68 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.79 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.242
Minimum - Maximum-1.1853836 - 2.2120495
Average (Standard dev.)0.0018249566 (±0.053056195)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions292292292
Spacing292292292
CellA=B=C: 230.68001 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_63823_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half B

Fileemd_63823_half_map_1.map
Annotationhalf B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half A

Fileemd_63823_half_map_2.map
Annotationhalf A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : human AC9 in complex with GalphaS

EntireName: human AC9 in complex with GalphaS
Components
  • Complex: human AC9 in complex with GalphaS
    • Protein or peptide: Adenylate cyclase type 9,Protein M2-1
    • Protein or peptide: Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
  • Ligand: 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE
  • Ligand: MAGNESIUM ION

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Supramolecule #1: human AC9 in complex with GalphaS

SupramoleculeName: human AC9 in complex with GalphaS / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 150 kDa/nm

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Macromolecule #1: Adenylate cyclase type 9,Protein M2-1

MacromoleculeName: Adenylate cyclase type 9,Protein M2-1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: adenylate cyclase
Source (natural)Organism: Human respiratory syncytial virus
Molecular weightTheoretical: 181.560188 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MASPPHQQLL HHHSTEVSCD SSGDSNSVRV KINPKQLSSN SHPKHCKYSI SSSCSSSGDS GGVPRRVGGG GRLRRQKKLP QLFERASSR WWDPKFDSVN LEEACLERCF PQTQRRFRYA LFYIGFACLL WSIYFAVHMR SRLIVMVAPA LCFLLVCVGF F LFTFTKLY ...String:
MASPPHQQLL HHHSTEVSCD SSGDSNSVRV KINPKQLSSN SHPKHCKYSI SSSCSSSGDS GGVPRRVGGG GRLRRQKKLP QLFERASSR WWDPKFDSVN LEEACLERCF PQTQRRFRYA LFYIGFACLL WSIYFAVHMR SRLIVMVAPA LCFLLVCVGF F LFTFTKLY ARHYAWTSLA LTLLVFALTL AAQFQVLTPV SGRGDSSNLT ATARPTDTCL SQVGSFSMCI EVLFLLYTVM HL PLYLSLC LGVAYSVLFE TFGYHFRDEA CFPSPGAGAL HWELLSRGLL HGCIHAIGVH LFVMSQVRSR STFLKVGQSI MHG KDLEVE KALKERMIHS VMPRIIADDL MKQGDEESEN SVKRHATSSP KNRKKKSSIQ KAPIAFRPFK MQQIEEVSIL FADI VGFTK MSANKSAHAL VGLLNDLFGR FDRLCEETKC EKISTLGDCY YCVAGCPEPR ADHAYCCIEM GLGMIKAIEQ FCQEK KEMV NMRVGVHTGT VLCGILGMRR FKFDVWSNDV NLANLMEQLG VAGKVHISEA TAKYLDDRYE MEDGKVIERL GQSVVA DQL KGLKTYLISG QRAKESRCSC AEALLSGFEV IDGSQVSSGP RGQGTASSGN VSDLAQTVKT FDNLKTCPSC GITFAPK SE AGAEGGAPQN GCQDEHKNST KASGGPNPKT QNGLLSPPQE EKLTNSQTSL CEILQEKGRW AGVSLDQSAL LPLRFKNI R EKTDAHFVDV IKEDSLMKDY FFKPPINQFS LNFLDQELER SYRTSYQEEV IKNSPVKTFA SPTFSSLLDV FLSTTVFLT LSTTCFLKYE AATVPPPPAA LAVFSAALLL EVLSLAVSIR MVFFLEDVMA CTKRLLEWIA GWLPRHCIGA ILVSLPALAV YSHVTSEYE TNIHFPVFTG SAALIAVVHY CNFCQLSSWM RSSLATVVGA GPLLLLYVSL CPDSSVLTSP LDAVQNFSSE R NPCNSSVP RDLRRPASLI GQEVVLVFFL LLLLVWFLNR EFEVSYRLHY HGDVEADLHR TKIQSMRDQA DWLLRNIIPY HV AEQLKVS QTYSKNHDSG GVIFASIVNF SEFYEENYEG GKECYRVLNE LIGDFDELLS KPDYSSIEKI KTIGATYMAA SGL NTAQAQ DGSHPQEHLQ ILFEFAKEMM RVVDDFNNNM LWFNFKLRVG FNHGPLTAGV IGTTKLLYDI WGDTVNIASR MDTT GVECR IQVSEESYRV LSKMGYDFDY RGTVNVKGKG QMKTYLYPKC TDHRVIPQHQ LSISPDIRVQ VDGSIGRSPT DEIAN LVPS VQYVDKTSLG SDSSTQAKDA HLSPKRPWKE PVKAEERGRF GKAIEKDDCD ETGIEEANEL TKLNVSKSVG SNSENL YFQ GSMVSKGEEL FTGVVPILVE LDGDVNGHKF SVSGEGEGDA TYGKLTLKFI CTTGKLPVPW PTLVTTLTYG VQCFSRY PD HMKQHDFFKS AMPEGYVQER TIFFKDDGNY KTRAEVKFEG DTLVNRIELK GIDFKEDGNI LGHKLEYNYN SHNVYIMA D KQKNGIKVNF KIRHNIEDGS VQLADHYQQN TPIGDGPVLL PDNHYLSTQS KLSKDPNEKR DHMVLLEFVT AAGITLGMD ELYKHHHHHH HHHHDYKDDD DK

UniProtKB: Adenylate cyclase type 9, Protein M2-1

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Macromolecule #2: Guanine nucleotide-binding protein G(s) subunit alpha isoforms short

MacromoleculeName: Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
EC number: Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 49.331168 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MGCLGNSKTE DQRNEEKAQR EANKKIEKQL QKDKQVYRAT HRLLLLGAGE SGKSTIVKQM RILHVNGFNG EGGEEDPQAA RSNSDGEKA TKVQDIKNNL KEAIETIVAA MSNLVPPVEL ANPENQFRVD YILSVMNVPD FDFPPEFYEH AKALWEDEGV R ACYERSNE ...String:
MGCLGNSKTE DQRNEEKAQR EANKKIEKQL QKDKQVYRAT HRLLLLGAGE SGKSTIVKQM RILHVNGFNG EGGEEDPQAA RSNSDGEKA TKVQDIKNNL KEAIETIVAA MSNLVPPVEL ANPENQFRVD YILSVMNVPD FDFPPEFYEH AKALWEDEGV R ACYERSNE YQLIDCAQYF LDKIDVIKQA DYVPSDQDLL RCRVLTSGIF ETKFQVDKVN FHMFDVGGQR DERRKWIQCF ND VTAIIFV VASSSYNMVI REDNQTNRLQ EALNLFKSIW NNRWLRTISV ILFLNKQDLL AEKVLAGKSK IEDYFPEFAR YTT PEDATP EPGEDPRVTR AKYFIRDEFL RISTASGDGR HYCYPHFTCA VDTENIRRVF NDCRDIIQRM HLRQYELLSN SENL YFQGS HHHHHHHHHH DYKDDDDK

UniProtKB: Guanine nucleotide-binding protein G(s) subunit alpha isoforms short

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Macromolecule #3: 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE

MacromoleculeName: 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE / type: ligand / ID: 3 / Number of copies: 1 / Formula: GSP
Molecular weightTheoretical: 539.246 Da
Chemical component information

ChemComp-GSP:
5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE

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Macromolecule #4: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 4 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeJEOL CRYO ARM 300
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.8 µm

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Image processing

CTF correctionType: PHASE FLIPPING ONLY
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.65 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 170990
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING
FSC plot (resolution estimation)

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