4Q66

Structure of Exomer bound to Arf1.

Summary for 4Q66

• Entry DOI: 10.2210/pdb4q66/pdb
• Related: 4GNS 4IN3
• Descriptor: Chs5p, Protein BCH1, ADP-ribosylation factor 1, ... (5 entities in total)
• Functional Keywords: cargo adaptor, secretory vesicle, small gtp-ase arf1-binding, trans-golgi network, protein transport
• Biological source: Saccharomyces cerevisiae R008 (Baker's yeast); More
• Cellular location: Golgi apparatus, trans-Golgi network membrane ; Peripheral membrane protein : Q05029; Golgi apparatus: P11076
• Total number of polymer chains: 12
• Total formula weight: 581631.24

Authors

Paczkowski, J.E.,Fromme, J.C. (deposition date: 2014-04-21, release date: 2014-09-17, Last modification date: 2024-02-28)

Primary citation

Paczkowski, J.E.,Fromme, J.C.
Structural basis for membrane binding and remodeling by the exomer secretory vesicle cargo adaptor.
Dev.Cell, 30:610-624, 2014

PubMed Abstract: Cargo adaptor subunits of vesicle coat protein complexes sort transmembrane proteins to distinct membrane compartments in eukaryotic cells. The exomer complex is the only cargo adaptor known to sort proteins at the trans-Golgi network into secretory vesicles. Exomer function is regulated by the Arf1 GTPase, a master regulator of trafficking at the Golgi. We report the structure of exomer bound to two copies of Arf1. Exomer interacts with each Arf1 molecule via two surfaces, one of which is a noncanonical interface that regulates GTP hydrolysis. The structure uncovers an unexpected membrane-proximal hydrophobic element that exomer uses in cooperation with Arf1 to remodel membranes. Given the constrained motion of the exomer hinge region, we envision that exomer dynamically positions multiple membrane insertion elements to drive membrane fission. In contrast to other known cargo adaptors, exomer therefore couples two functions, cargo sorting and membrane fission, into a single complex.

PubMed: 25203211
DOI: 10.1016/j.devcel.2014.07.014

Experimental method

X-RAY DIFFRACTION (3.354 Å)