6JL7

crystal structure of TBC1D23 N terminal domain

Summary for 6JL7

• Entry DOI: 10.2210/pdb6jl7/pdb
• Descriptor: TBC1 domain family member 23 (2 entities in total)
• Functional Keywords: vesicle transport, bridging factor, protein transport
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 50487.86

Authors

Sun, Q.,Hu, W.,Jia, D. (deposition date: 2019-03-04, release date: 2020-03-04, Last modification date: 2024-11-13)

Primary citation

Liu, D.,Yang, F.,Liu, Z.,Wang, J.,Huang, W.,Meng, W.,Billadeau, D.D.,Sun, Q.,Mo, X.,Jia, D.
Structure of TBC1D23 N-terminus reveals a novel role for rhodanese domain.
Plos Biol., 18:e3000746-e3000746, 2020

PubMed Abstract: Members of the Tre2-Bub2-Cdc16 (TBC) family often function to regulate membrane trafficking and to control signaling transductions pathways. As a member of the TBC family, TBC1D23 is critical for endosome-to-Golgi cargo trafficking by serving as a bridge between Golgi-bound golgin-97/245 and the WASH/FAM21 complex on endosomal vesicles. However, the exact mechanisms by which TBC1D23 regulates cargo transport are poorly understood. Here, we present the crystal structure of the N-terminus of TBC1D23 (D23N), which consists of both the TBC and rhodanese domains. We show that the rhodanese domain is unlikely to be an active sulfurtransferase or phosphatase, despite containing a putative catalytic site. Instead, it packs against the TBC domain and forms part of the platform to interact with golgin-97/245. Using the zebrafish model, we show that impacting golgin-97/245-binding, but not the putative catalytic site, impairs neuronal growth and brain development. Altogether, our studies provide structural and functional insights into an essential protein that is required for organelle-specific trafficking and brain development.

PubMed: 32453802
DOI: 10.1371/journal.pbio.3000746

Experimental method

X-RAY DIFFRACTION (2.5 Å)