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Crystal structure of yeast alpha/betaprime-COP subcomplex of the COPI vesicular coatCrystal structure of yeast alpha/betaprime-COP subcomplex of the COPI vesicular coat
Structural highlights
Function[COPA_YEAST] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCOPI-coated vesicles form at the Golgi apparatus from two cytosolic components, ARF G protein and coatomer, a heptameric complex that can polymerize into a cage to deform the membrane into a bud. Although coatomer shares a common evolutionary origin with COPII and clathrin vesicle coat proteins, the architectural relationship among the three cages is unclear. Strikingly, the alphabeta'-COP core of coatomer crystallizes as a triskelion in which three copies of a beta'-COP beta-propeller domain converge through their axial ends. We infer that the trimer constitutes the vertex of the COPI cage. Our model proposes that the COPI cage is intermediate in design between COPII and clathrin: COPI shares with clathrin an arrangement of three curved alpha-solenoid legs radiating from a common center, and COPI shares with COPII highly similar vertex interactions involving the axial ends of beta-propeller domains. Structure of coatomer cage proteins and the relationship among COPI, COPII, and clathrin vesicle coats.,Lee C, Goldberg J Cell. 2010 Jul 9;142(1):123-32. Epub 2010 Jun 24. PMID:20579721[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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