1TBG

BETA-GAMMA DIMER OF THE HETEROTRIMERIC G-PROTEIN TRANSDUCIN

Summary for 1TBG

• Entry DOI: 10.2210/pdb1tbg/pdb
• Descriptor: TRANSDUCIN (3 entities in total)
• Functional Keywords: complex (gtp-binding-transducer), eye, transducer, prenylation, complex (gtp-binding-transducer) complex, complex (gtp-binding/transducer)
• Biological source: Bos taurus (cattle); More
• Cellular location: Cell membrane; Lipid-anchor; Cytoplasmic side (Potential): P02698
• Total number of polymer chains: 8
• Total formula weight: 181588.46

Authors

Sondek, J.S.,Bohm, A.,Lambright, D.G.,Hamm, H.E.,Sigler, P.B. (deposition date: 1996-06-15, release date: 1997-04-01, Last modification date: 2024-02-14)

Primary citation

Sondek, J.,Bohm, A.,Lambright, D.G.,Hamm, H.E.,Sigler, P.B.
Crystal structure of a G-protein beta gamma dimer at 2.1A resolution.
Nature, 379:369-374, 1996

PubMed Abstract: 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.

PubMed: 8552196
DOI: 10.1038/379369a0

Experimental method

X-RAY DIFFRACTION (2.1 Å)