This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. This is the third in a series of proposals that aims at obtaining structural information on the yeast COPII vesicalar coat. COPII is a 420 kDa pentameric complex responsible for budding transport vesicles from the endoplasmic reticulum (ER) and delivering the specific cargo contents to the Golgi complex. In the first proposal we focused on the inner shell of the COPII coat, the Sec23/24-Sar1 complex. We were able to determine the structures of three complexes of Sec24 bond to cargo and SNARE sequences (paper published in Cell). In the current proposal we focus on the outer shell of COPII , comprising of the Sec13/31 complex. Sec 13/31 is functionally, but not structurally, homolosous to clathrin--it polymerizes the COPII inner shell on the ER membrane and causes membrane deformation. Since, like clathrin, Sec13/31 is a long, flexible structure capable of oligomerizing (as seen in EM images) it is unlikely that the intact complex can be crystallized. There fore, we have dessected the protein into waht we believe are the tow functionally interesting fragments, and these constitue the two projects that we propose in this application.
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