Unusual armadillo fold in the human general vesicular transport factor p115

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Item Type:	Article
Title:	Unusual armadillo fold in the human general vesicular transport factor p115
Creators Name:	Striegl, H., Roske, Y., Kuemmel, D. and Heinemann, U.
Abstract:	The golgin family gives identity and structure to the Golgi apparatus and is part of a complex protein network at the Golgi membrane. The golgin p115 is targeted by the GTPase Rab1a, contains a large globular head region and a long region of coiled-coil which forms an extended rod-like structure. p115 serves as vesicle tethering factor and plays an important role at different steps of vesicular transport. Here we present the 2.2 A-resolution X-ray structure of the globular head region of p115. The structure exhibits an armadillo fold that is decorated by elongated loops and carries a C-terminal non-canonical repeat. This terminal repeat folds into the armadillo superhelical groove and allows homodimeric association with important implications for p115 mediated multiple protein interactions and tethering.
Keywords:	Amino Acid Sequence, X-Ray Crystallography, Molecular Models, Molecular Sequence Data, Protein Conformation, Protein Folding, Amino Acid Sequence Homology, Vesicular Transport Proteins
Source:	PLoS ONE
ISSN:	1932-6203
Publisher:	Public Library of Science
Volume:	4
Number:	2
Page Range:	e4656
Date:	27 February 2009
Official Publication:	https://doi.org/10.1371/journal.pone.0004656
PubMed:	View item in PubMed

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