2pm9 | pdb_00002pm9
From Proteopedia
Crystal structure of yeast Sec13/31 vertex element of the COPII vesicular coat
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Structural highlights
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 PubMedCOPII-coated vesicles export newly synthesized proteins from the endoplasmic reticulum. The COPII coat consists of the Sec23/24-Sar1 complex that selects cargo and the Sec13/31 assembly unit that can polymerize into an octahedral cage and deform the membrane into a bud. Crystallographic analysis of the assembly unit reveals a 28 nm long rod comprising a central alpha-solenoid dimer capped by two beta-propeller domains at each end. We construct a molecular model of the COPII cage by fitting Sec13/31 crystal structures into a recently determined electron microscopy density map. The vertex geometry involves four copies of the Sec31 beta-propeller that converge through their axial ends; there is no interdigitation of assembly units of the kind seen in clathrin cages. We also propose that the assembly unit has a central hinge-an arrangement of interlocked alpha-solenoids-about which it can bend to adapt to cages of variable curvature. Structure and organization of coat proteins in the COPII cage.,Fath S, Mancias JD, Bi X, Goldberg J Cell. 2007 Jun 29;129(7):1325-36. PMID:17604721[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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