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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. and Roske, Y. and 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 (U.S.A.)
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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