![]() ![]() The Trs130 subunit provides a “leg” that positions the active site distal to the membrane surface, and this leg is required for steric gating. Here, we present cryo–electron microscopy structures of the 22-subunit TRAPPII complex from budding yeast, including a TRAPPII-Rab11 nucleotide exchange intermediate. A steric gating mechanism has been proposed to explain TRAPPII counterselection against Rab1. ![]() The basal specificity of the TRAPP core is toward Rab1, yet the TRAPPII complex is specific for Rab11. The transport protein particle (TRAPP) complexes activate these guanosine triphosphatases via nucleotide exchange using a shared set of core subunits. Rab1 and Rab11 are essential regulators of the eukaryotic secretory and endocytic recycling pathways.
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