3pr6
From Proteopedia
Crystal structure analysis of yeast TRAPP associate protein Tca17
Structural highlights
FunctionTCA17_YEAST Required, together with the TRAPP II subunit TRS33, for TRAPP II complex assembly or stability, and for proper Golgi localization of TRAPP and the Rab GTPase YPT31.[1] [2] Publication Abstract from PubMedThe 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 A. 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. This article is protected by copyright. All rights reserved. Crystal structure of the yeast TRAPP-associated protein Tca17.,Wang C, Gohlke U, Roske Y, Heinemann U FEBS J. 2014 Jun 24. doi: 10.1111/febs.12888. PMID:24961828[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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