Structure and organization of coat proteins in the COPII cage. Export

@article{citeulike:2770881, abstract = {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.}, address = {Howard Hughes Medical Institute and the Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.}, author = {Fath, S. and Mancias, J. D. and Bi, X. and Goldberg, J.}, citeulike-article-id = {2770881}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.cell.2007.05.036}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0092867407006757}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/17604721}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=17604721}, day = {29}, doi = {10.1016/j.cell.2007.05.036}, issn = {0092-8674}, journal = {Cell}, keywords = {copii, sec13, sec31}, month = {June}, number = {7}, pages = {1325--1336}, posted-at = {2009-05-13 12:21:29}, priority = {2}, title = {Structure and organization of coat proteins in the COPII cage.}, url = {http://dx.doi.org/10.1016/j.cell.2007.05.036}, volume = {129}, year = {2007} }

TY - JOUR ID - citeulike:2770881 L3 - citeulike-article-id:2770881 N2 - 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. IS - 7 JF - Cell SN - 0092-8674 AD - Howard Hughes Medical Institute and the Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA. EP - 1336 TI - Structure and organization of coat proteins in the COPII cage. VL - 129 SP - 1325 KW - copii KW - sec13 KW - sec31 AU - Fath, S AU - Mancias, JD AU - Bi, X AU - Goldberg, J PY - 2007/06/29/ UR - http://dx.doi.org/10.1016/j.cell.2007.05.036 ER -