4J87

Crystal structure of alpha-COP

Summary for 4J87

• Entry DOI: 10.2210/pdb4j87/pdb
• Related: 4J73 4J77 4J78 4J79 4J81 4J82 4J84 4J86 4J8B 4J8G
• Descriptor: coatomer subunit alpha (2 entities in total)
• Functional Keywords: beta propeller domain, vesicle trafficking, protein transport
• Biological source: Schizosaccharomyces pombe (Fission yeast)
• Cellular location: Cytoplasm: Q96WV5
• Total number of polymer chains: 1
• Total formula weight: 37525.86

Authors

Ma, W.,Goldberg, J. (deposition date: 2013-02-14, release date: 2013-03-27, Last modification date: 2024-02-28)

Primary citation

Ma, W.,Goldberg, J.
Rules for the recognition of dilysine retrieval motifs by coatomer.
Embo J., 32:926-937, 2013

PubMed Abstract: Cytoplasmic dilysine motifs on transmembrane proteins are captured by coatomer α-COP and β'-COP subunits and packaged into COPI-coated vesicles for Golgi-to-ER retrieval. Numerous ER/Golgi proteins contain K(x)Kxx motifs, but the rules for their recognition are unclear. We present crystal structures of α-COP and β'-COP bound to a series of naturally occurring retrieval motifs-encompassing KKxx, KxKxx and non-canonical RKxx and viral KxHxx sequences. Binding experiments show that α-COP and β'-COP have generally the same specificity for KKxx and KxKxx, but only β'-COP recognizes the RKxx signal. Dilysine motif recognition involves lysine side-chain interactions with two acidic patches. Surprisingly, however, KKxx and KxKxx motifs bind differently, with their lysine residues transposed at the binding patches. We derive rules for retrieval motif recognition from key structural features: the reversed binding modes, the recognition of the C-terminal carboxylate group which enforces lysine positional context, and the tolerance of the acidic patches for non-lysine residues.

PubMed: 23481256
DOI: 10.1038/emboj.2013.41

Experimental method

X-RAY DIFFRACTION (1.67 Å)