1AZS

COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.282 
  • R-Value Work: 0.219 
  • R-Value Observed: 0.219 

Starting Model: experimental
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Literature

Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS.

Tesmer, J.J., Sunahara, R.K., Gilman, A.G., Sprang, S.R.

(1997) Science 278: 1907-1916

  • DOI: https://doi.org/10.1126/science.278.5345.1907
  • Primary Citation of Related Structures:  
    1AZS

  • PubMed Abstract: 

    The crystal structure of a soluble, catalytically active form of adenylyl cyclase in a complex with its stimulatory heterotrimeric G protein alpha subunit (Gsalpha) and forskolin was determined to a resolution of 2.3 angstroms. When P-site inhibitors were soaked into native crystals of the complex, the active site of adenylyl cyclase was located and structural elements important for substrate recognition and catalysis were identified. On the basis of these and other structures, a molecular mechanism is proposed for the activation of adenylyl cyclase by Gsalpha.

    • Organizational Affiliation: 

    Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75235-9050, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
VC1220Canis lupus familiarisMutation(s): 1 
Gene Names: ADENYLYL CYCLASE TYPE V
EC: 4.6.1.1
UniProt
Find proteins for P30803 (Canis lupus familiaris)
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Go to UniProtKB:  P30803
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UniProt GroupP30803
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
IIC2212Rattus norvegicusMutation(s): 0 
Gene Names: ADENYLYL CYCLASE TYPE II
EC: 4.6.1.1
UniProt
Find proteins for P26769 (Rattus norvegicus)
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Go to UniProtKB:  P26769
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UniProt GroupP26769
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
GS-ALPHA402Bos taurusMutation(s): 0 
Gene Names: GNAS
EC: 3.6.5
UniProt
Find proteins for P04896 (Bos taurus)
Explore P04896 
Go to UniProtKB:  P04896
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UniProt GroupP04896
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.282 
  • R-Value Work: 0.219 
  • R-Value Observed: 0.219 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 119α = 90
b = 134.05β = 90
c = 70.65γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
X-PLORrefinement
DENZOdata reduction
SCALEPACKdata scaling
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-02-25
    Type: Initial release
  • Version 1.1: 2008-03-03
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2021-11-03
    Changes: Database references, Derived calculations, Other
  • Version 1.4: 2023-08-02
    Changes: Refinement description
  • Version 1.5: 2024-05-22
    Changes: Data collection