2TRC

PHOSDUCIN/TRANSDUCIN BETA-GAMMA COMPLEX

Summary for 2TRC

• Entry DOI: 10.2210/pdb2trc/pdb
• Descriptor: TRANSDUCIN, PHOSDUCIN, GADOLINIUM ATOM, ... (5 entities in total)
• Functional Keywords: phosducin, transducin, beta-gamma, signal transduction, regulation, phosphorylation, g proteins, thioredoxin, vision, meka, complex (transducer-transduction), complex (transducer-transduction) complex, complex (transducer/transduction)
• Biological source: Rattus norvegicus (Norway rat); More
• Total number of polymer chains: 3
• Total formula weight: 71345.91

Authors

Gaudet, R.,Bohm, A.,Sigler, P.B. (deposition date: 1997-01-06, release date: 1997-06-05, Last modification date: 2019-08-14)

Primary citation

Gaudet, R.,Bohm, A.,Sigler, P.B.
Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin.
Cell(Cambridge,Mass.), 87:577-588, 1996

PubMed Abstract: The crystal structure of transducin's betagamma subunits complexed with phosducin, which regulates Gtbetagamma activity, has been solved to 2.4 angstroms resolution. Phosducin has two domains that wrap around Gtbetagamma to form an extensive interface. The N-terminal domain binds loops on the "top" Gtbeta surface, overlapping the Gtalpha binding surface, explaining how phosducin blocks Gtbetagamma's interaction with Gtalpha. The C-terminal domain shows structural homology to thioredoxin and binds the outer strands of Gtbeta's seventh and first blades in a manner likely to disrupt Gtbetagamma's normal orientation relative to the membrane and receptor. Phosducin's Ser-73, which when phosphorylated inhibits phosducin's function, points away from Gtbetagamma, toward a large flexible loop. Thus phosphorylation is not likely to affect the interface directly, but rather indirectly through an induced conformational change.

PubMed: 8898209
DOI: 10.1016/S0092-8674(00)81376-8

Experimental method

X-RAY DIFFRACTION (2.4 Å)