4IN3

Crystal Structure of the Chs5-Bch1 Exomer Cargo Adaptor Complex

Summary for 4IN3

• Entry DOI: 10.2210/pdb4in3/pdb
• Descriptor: Chitin biosynthesis protein CHS5, Protein BCH1 (3 entities in total)
• Functional Keywords: ob fold, tpr domain, trans-golgi network, tgn, protein transport
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Golgi apparatus, trans-Golgi network membrane ; Peripheral membrane protein : Q12114 Q05029
• Total number of polymer chains: 4
• Total formula weight: 186490.03

Authors

Richardson, B.C.,Fromme, J.C. (deposition date: 2013-01-03, release date: 2013-03-06, Last modification date: 2023-09-20)

Primary citation

Richardson, B.C.,Fromme, J.C.
The exomer cargo adaptor features a flexible hinge domain.
Structure, 21:486-492, 2013

PubMed Abstract: Exomer is a cargo adaptor that mediates the sorting of specific plasma membrane proteins into vesicles at the trans-Golgi network. Cargo adaptors must bind to multiple partners, including their cargo, regulatory proteins, and the membrane surface. During biogenesis of a vesicle, the membrane makes a transition from a relatively flat surface to one of high curvature, requiring cargo adaptors to somehow maintain protein-protein and protein-membrane interactions on a changing membrane environment. Here, we present the crystal structure of a tetrameric Chs5/Bch1 exomer complex and use small-angle X-ray scattering to demonstrate its flexibility in solution. The structural data suggest that the complex flexes primarily around the dimeric N-terminal domain of the Chs5 subunits, which adopts a noncanonical β sandwich fold. We propose that this flexible hinge domain enables exomer to maintain interactions in the context of a dynamic membrane environment.

PubMed: 23395181
DOI: 10.1016/j.str.2013.01.003

Experimental method

X-RAY DIFFRACTION (2.936 Å)