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Crystal structure of the yeast TRAPP-associated protein Tca17

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Item Type:Article
Title:Crystal structure of the yeast TRAPP-associated protein Tca17
Creators Name:Wang, C. and Gohlke, U. and Roske, Y. and Heinemann, U.
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 {Angstrom}. 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.
Keywords:Sedlin, Tca17, TRAPP, Trs20, Vesicle Transport
Source:FEBS Journal
ISSN:1742-464X
Publisher:Wiley-Blackwell (U.K.)
Volume:281
Number:18
Page Range:4195-4206
Date:September 2014
Official Publication:https://doi.org/10.1111/febs.12888
PubMed:View item in PubMed

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