Unknown

Dataset Information

0

The exomer cargo adaptor features a flexible hinge domain.


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 ? sandwich fold. We propose that this flexible hinge domain enables exomer to maintain interactions in the context of a dynamic membrane environment.

SUBMITTER: Richardson BC 

PROVIDER: S-EPMC3957094 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

The exomer cargo adaptor features a flexible hinge domain.

Richardson Brian C BC   Fromme J Christopher JC  

Structure (London, England : 1993) 20130207 3


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.  ...[more]

Similar Datasets

| S-EPMC3492730 | biostudies-literature
| S-EPMC5290816 | biostudies-other
| S-EPMC4159615 | biostudies-literature
| S-EPMC5887143 | biostudies-literature
| S-EPMC4207043 | biostudies-literature
| S-EPMC3663503 | biostudies-literature
| S-EPMC7147021 | biostudies-literature
| S-EPMC2592659 | biostudies-literature
| S-EPMC3970527 | biostudies-literature
| S-EPMC5866929 | biostudies-literature