Structure and Organization of Coat Proteins in the COPll Cage
COPII-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.
- Research Organization:
- Brookhaven National Laboratory (BNL) National Synchrotron Light Source
- Sponsoring Organization:
- Doe - Office Of Science
- DOE Contract Number:
- AC02-98CH10886
- OSTI ID:
- 930476
- Report Number(s):
- BNL--81228-2008-JA
- Journal Information:
- Cell, Journal Name: Cell Journal Issue: 7 Vol. 129; ISSN 0092-8674; ISSN CELLB5
- Country of Publication:
- United States
- Language:
- English
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