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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...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2009
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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. |
format | Text |
id | pubmed-2645507 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
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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