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.
Copyright © 2013 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Binding Sites
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Chitin Synthase / chemistry*
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Chitin Synthase / genetics
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Crystallography, X-Ray
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Escherichia coli / genetics
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Kinetics
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Membrane Glycoproteins / chemistry*
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Membrane Glycoproteins / genetics
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Molecular Dynamics Simulation
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Mutation
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Protein Binding
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Protein Folding
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Protein Multimerization
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Protein Subunits / chemistry*
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Protein Subunits / genetics
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Protein Transport
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Saccharomyces cerevisiae / chemistry*
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae Proteins / chemistry*
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Saccharomyces cerevisiae Proteins / genetics
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Structure-Activity Relationship
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Thermodynamics
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trans-Golgi Network / chemistry
Substances
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Membrane Glycoproteins
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Protein Subunits
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Recombinant Proteins
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Saccharomyces cerevisiae Proteins
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CHS5 protein, S cerevisiae
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Chitin Synthase