Crystal structure of a G-protein beta gamma dimer at 2.1A resolution

Nature. 1996 Jan 25;379(6563):369-74. doi: 10.1038/379369a0.


Many signalling cascades use seven-helical transmembrane receptors coupled to heterotrimeric G proteins (G alpha beta gamma) to convert extracellular signals into intracellular responses. Upon nucleotide exchange catalysed by activated receptors, heterotrimers dissociate into GTP-bound G alpha subunits and G beta gamma dimers, either of which can modulate many downstream effectors. Here we use multiwavelength anomalous diffraction data to solve the crystal structure of the beta gamma dimer of the G protein transducin. The beta-subunit is primarily a seven-bladed beta-propeller that is partially encircled by an extended gamma-subunit. The beta-propeller, which contains seven structurally similar WD repeats, defines the stereochemistry of the WD repeat and the probable architecture of all WD-repeat-containing domains. The structure details interactions between G protein beta- and gamma-subunits and highlights regions implicated in effector modulation for the conserved family of G protein beta gamma dimers.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Crystallography, X-Ray
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Retinal Rod Photoreceptor Cells / chemistry
  • Sequence Homology, Amino Acid
  • Transducin / chemistry*


  • Transducin

Associated data

  • GENBANK/L34290
  • SWISSPROT/P02698
  • SWISSPROT/P04901
  • SWISSPROT/P11016
  • SWISSPROT/P16520
  • SWISSPROT/P16874
  • SWISSPROT/P17343
  • SWISSPROT/P18851
  • SWISSPROT/P18852
  • SWISSPROT/P26308
  • SWISSPROT/P29387
  • SWISSPROT/P29798
  • SWISSPROT/P29829
  • SWISSPROT/P30670
  • SWISSPROT/P30671
  • SWISSPROT/P36408
  • SWISSPROT/P38040
  • SWISSPROT/Q01821
  • SWISSPROT/Q08447