3PR6

Crystal structure analysis of yeast TRAPP associate protein Tca17

Summary for 3PR6

• Entry DOI: 10.2210/pdb3pr6/pdb
• Descriptor: TRAPP-associated protein TCA17, CHLORIDE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: longin fold, vesicle tethering regulation, trapp complex, trans-golgi network, transport protein
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Golgi apparatus, trans-Golgi network : P32613
• Total number of polymer chains: 1
• Total formula weight: 18480.17

Authors

Wang, C.,Gohlke, U.,Heinemann, U. (deposition date: 2010-11-29, release date: 2011-11-30, Last modification date: 2024-11-27)

Primary citation

Wang, C.,Gohlke, U.,Roske, Y.,Heinemann, U.
Crystal structure of the yeast TRAPP-associated protein Tca17.
Febs J., 281:4195-4206, 2014

PubMed Abstract: The transport protein particle (TRAPP) is a hetero-multimeric complex involved in the trafficking of COP II (coat protein complex II) vesicles. TRAPP is present in different eukaryotes from yeast to vertebrates and occurs in three distinct modifications with function in different intracellular transport steps. All forms contain a core of five essential subunits, and the different species of TRAPP are formed by the addition of various subunits. A recently identified TRAPP-associated protein, Tca17, is supposed to be involved in the regulation of the transport complex. We have determined the three-dimensional structure of yeast Tca17 by X-ray crystallography at a resolution of 1.8 Å. It adopts the longin fold characteristic for the Bet5 family of TRAPP subunits, and it also shares a binding motif of these for the interaction with other members of the complex. Two alternative models of the localization of Tca17 within TRAPP as well as its potential role in the regulation of TRAPP function by transient integration into the complex are discussed.

PubMed: 24961828
DOI: 10.1111/febs.12888

Experimental method

X-RAY DIFFRACTION (1.8 Å)