7E2C

Monomer of TRAPPII (open)

Summary for 7E2C

• Entry DOI: 10.2210/pdb7e2c/pdb
• EMDB information: 30954
• Descriptor: TRAPP-associated protein TCA17, Trafficking protein particle complex II-specific subunit 65, Trafficking protein particle complex subunit 33, ... (10 entities in total)
• Functional Keywords: protein transport trappii open, protein transport
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 11
• Total formula weight: 526759.84

Authors

Sui, S.F.,Sun, S.,Mi, C.C. (deposition date: 2021-02-05, release date: 2022-02-09, Last modification date: 2024-06-05)

Primary citation

Mi, C.,Zhang, L.,Huang, G.,Shao, G.,Yang, F.,You, X.,Dong, M.Q.,Sun, S.,Sui, S.F.
Structural basis for assembly of TRAPPII complex and specific activation of GTPase Ypt31/32.
Sci Adv, 8:eabi5603-eabi5603, 2022

PubMed Abstract: Transport protein particle (TRAPP) complexes belong to the multiprotein tethering complex and exist in three forms-core TRAPP/TRAPPI, TRAPPII, and TRAPPIII. TRAPPII activates GTPase Ypt31/Ypt32 as the guanine nucleotide exchange factor in the trans-Golgi network to determine the maturation of Golgi cisternae into post-Golgi carriers in yeast. Here, we present cryo-EM structures of yeast TRAPPII in apo and Ypt32-bound states. All the structures show a dimeric architecture assembled by two triangle-shaped monomers, while the monomer in the apo state exhibits both open and closed conformations, and the monomer in the Ypt32-bound form only captures the closed conformation. Located in the interior of the monomer, Ypt32 binds with both core TRAPP/TRAPPI and Trs120 via its nucleotide-binding domain and binds with Trs31 via its hypervariable domain. Combined with functional analysis, the structures provide insights into the assembly of TRAPPII and the mechanism of the specific activation of Ypt31/Ypt32 by TRAPPII.

PubMed: 35080977
DOI: 10.1126/sciadv.abi5603

Experimental method

ELECTRON MICROSCOPY (4.18 Å)