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PDBsum entry 4yg8
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Transport protein
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PDB id
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4yg8
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References listed in PDB file
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Key reference
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Title
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The exomer cargo adaptor structure reveals a novel gtpase-Binding domain.
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Authors
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J.E.Paczkowski,
B.C.Richardson,
A.M.Strassner,
J.C.Fromme.
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Ref.
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Embo J, 2012,
31,
4191-4203.
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PubMed id
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Abstract
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Cargo adaptors control intracellular trafficking of transmembrane proteins by
sorting them into membrane transport carriers. The COPI, COPII, and clathrin
cargo adaptors are structurally well characterized, but other cargo adaptors
remain poorly understood. Exomer is a specialized cargo adaptor that sorts
specific proteins into trans-Golgi network (TGN)-derived vesicles in response to
cellular signals. Exomer is recruited to the TGN by the Arf1 GTPase, a
universally conserved trafficking regulator. Here, we report the crystal
structure of a tetrameric exomer complex composed of two copies each of the Chs5
and Chs6 subunits. The structure reveals the FN3 and BRCT domains of Chs5, which
together we refer to as the FBE domain (FN3-BRCT of exomer), project from the
exomer core complex. The overall architecture of the FBE domain is reminiscent
of the appendage domains of other cargo adaptors, although it exhibits a
distinct topology. In contrast to appendage domains, which bind accessory
factors, we show that the primary role of the FBE domain is to bind Arf1 for
recruitment of exomer to membranes.
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