7U05

Structure of the yeast TRAPPII-Rab11/Ypt32 complex in the closed/closed state (composite structure)

This is a non-PDB format compatible entry.

Summary for 7U05

• Entry DOI: 10.2210/pdb7u05/pdb
• EMDB information: 26221 26223 26224 26225 26226 26227 26228 26229 26230 26231 26232 26254
• Descriptor: Trafficking protein particle complex II-specific subunit 130, GTP-binding protein YPT32/YPT11, Trafficking protein particle complex II-specific subunit 120, ... (14 entities in total)
• Functional Keywords: complex, gtpase, guanosine exchange factor, gef, protein transport
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Total number of polymer chains: 28
• Total formula weight: 1182578.73

Authors

Bagde, S.R.,Fromme, J.C. (deposition date: 2022-02-17, release date: 2022-04-27, Last modification date: 2024-10-16)

Primary citation

Bagde, S.R.,Fromme, J.C.
Structure of a TRAPPII-Rab11 activation intermediate reveals GTPase substrate selection mechanisms.
Sci Adv, 8:eabn7446-eabn7446, 2022

PubMed Abstract: Rab1 and Rab11 are essential regulators of the eukaryotic secretory and endocytic recycling pathways. The transport protein particle (TRAPP) complexes activate these guanosine triphosphatases via nucleotide exchange using a shared set of core subunits. The basal specificity of the TRAPP core is toward Rab1, yet the TRAPPII complex is specific for Rab11. A steric gating mechanism has been proposed to explain TRAPPII counterselection against Rab1. Here, we present cryo-electron microscopy structures of the 22-subunit TRAPPII complex from budding yeast, including a TRAPPII-Rab11 nucleotide exchange intermediate. The Trs130 subunit provides a "leg" that positions the active site distal to the membrane surface, and this leg is required for steric gating. The related TRAPPIII complex is unable to activate Rab11 because of a repulsive interaction, which TRAPPII surmounts using the Trs120 subunit as a "lid" to enclose the active site. TRAPPII also adopts an open conformation enabling Rab11 to access and exit from the active site chamber.

PubMed: 35559680
DOI: 10.1126/sciadv.abn7446

Experimental method

ELECTRON MICROSCOPY (3.7 Å)