7UTH

Gea2 open/open conformation (composite structure)

Summary for 7UTH

• Entry DOI: 10.2210/pdb7uth/pdb
• Related: 7URO 7URR
• EMDB information: 26749 26750 26751 26752 26753 26754 26755 26765 26766 26769 26770 26771
• Descriptor: GEA2 isoform 1 (1 entity in total)
• Functional Keywords: gef, protein transport
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 331693.69

Authors

Muccini, A.,Fromme, J.C. (deposition date: 2022-04-26, release date: 2022-08-24, Last modification date: 2024-06-12)

Primary citation

Muccini, A.J.,Gustafson, M.A.,Fromme, J.C.
Structural basis for activation of Arf1 at the Golgi complex.
Cell Rep, 40:111282-111282, 2022

PubMed Abstract: The Golgi complex is the central sorting station of the eukaryotic secretory pathway. Traffic through the Golgi requires activation of Arf guanosine triphosphatases that orchestrate cargo sorting and vesicle formation by recruiting an array of effector proteins. Arf activation and Golgi membrane association is controlled by large guanine nucleotide exchange factors (GEFs) possessing multiple conserved regulatory domains. Here we present cryoelectron microscopy (cryoEM) structures of full-length Gea2, the yeast paralog of the human Arf-GEF GBF1, that reveal the organization of these regulatory domains and explain how Gea2 binds to the Golgi membrane surface. We find that the GEF domain adopts two different conformations compatible with different stages of the Arf activation reaction. The structure of a Gea2-Arf1 activation intermediate suggests that the movement of the GEF domain primes Arf1 for membrane insertion upon guanosine triphosphate binding. We propose that conformational switching of Gea2 during the nucleotide exchange reaction promotes membrane insertion of Arf1.

PubMed: 36044848
DOI: 10.1016/j.celrep.2022.111282

Experimental method

ELECTRON MICROSCOPY (3.9 Å)