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Unusual Armadillo Fold in the Human General Vesicular Transport Factor p115

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. p1...

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Detalles Bibliográficos
Autores principales: Striegl, Harald, Roske, Yvette, Kümmel, Daniel, Heinemann, Udo
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2645507/
https://www.ncbi.nlm.nih.gov/pubmed/19247479
http://dx.doi.org/10.1371/journal.pone.0004656
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author Striegl, Harald
Roske, Yvette
Kümmel, Daniel
Heinemann, Udo
author_facet Striegl, Harald
Roske, Yvette
Kümmel, Daniel
Heinemann, Udo
author_sort Striegl, Harald
collection PubMed
description 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 Å-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.
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spelling pubmed-26455072009-02-27 Unusual Armadillo Fold in the Human General Vesicular Transport Factor p115 Striegl, Harald Roske, Yvette Kümmel, Daniel Heinemann, Udo PLoS One Research Article 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 Å-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. Public Library of Science 2009-02-27 /pmc/articles/PMC2645507/ /pubmed/19247479 http://dx.doi.org/10.1371/journal.pone.0004656 Text en Striegl et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Striegl, Harald
Roske, Yvette
Kümmel, Daniel
Heinemann, Udo
Unusual Armadillo Fold in the Human General Vesicular Transport Factor p115
title Unusual Armadillo Fold in the Human General Vesicular Transport Factor p115
title_full Unusual Armadillo Fold in the Human General Vesicular Transport Factor p115
title_fullStr Unusual Armadillo Fold in the Human General Vesicular Transport Factor p115
title_full_unstemmed Unusual Armadillo Fold in the Human General Vesicular Transport Factor p115
title_short Unusual Armadillo Fold in the Human General Vesicular Transport Factor p115
title_sort unusual armadillo fold in the human general vesicular transport factor p115
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2645507/
https://www.ncbi.nlm.nih.gov/pubmed/19247479
http://dx.doi.org/10.1371/journal.pone.0004656
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