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ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions
The ESTHER database, which is freely available via a web server (http://bioweb.ensam.inra.fr/esther) and is widely used, is dedicated to proteins with an α/β-hydrolase fold, and it currently contains >30 000 manually curated proteins. Herein, we report those substantial changes towards improvemen...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3531081/ https://www.ncbi.nlm.nih.gov/pubmed/23193256 http://dx.doi.org/10.1093/nar/gks1154 |
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author | Lenfant, Nicolas Hotelier, Thierry Velluet, Eric Bourne, Yves Marchot, Pascale Chatonnet, Arnaud |
author_facet | Lenfant, Nicolas Hotelier, Thierry Velluet, Eric Bourne, Yves Marchot, Pascale Chatonnet, Arnaud |
author_sort | Lenfant, Nicolas |
collection | PubMed |
description | The ESTHER database, which is freely available via a web server (http://bioweb.ensam.inra.fr/esther) and is widely used, is dedicated to proteins with an α/β-hydrolase fold, and it currently contains >30 000 manually curated proteins. Herein, we report those substantial changes towards improvement that we have made to improve ESTHER during the past 8 years since our 2004 update. In particular, we generated 87 new families and increased the coverage of the UniProt Knowledgebase (UniProtKB). We also renewed the ESTHER website and added new visualization tools, such as the Overall Table and the Family Tree. We also address two topics of particular interest to the ESTHER users. First, we explain how the different enzyme classifications (bacterial lipases, peptidases, carboxylesterases) used by different communities of users are combined in ESTHER. Second, we discuss how variations of core architecture or in predicted active site residues result in a more precise clustering of families, and whether this strategy provides trustable hints to identify enzyme-like proteins with no catalytic activity. |
format | Online Article Text |
id | pubmed-3531081 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-35310812013-03-07 ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions Lenfant, Nicolas Hotelier, Thierry Velluet, Eric Bourne, Yves Marchot, Pascale Chatonnet, Arnaud Nucleic Acids Res Articles The ESTHER database, which is freely available via a web server (http://bioweb.ensam.inra.fr/esther) and is widely used, is dedicated to proteins with an α/β-hydrolase fold, and it currently contains >30 000 manually curated proteins. Herein, we report those substantial changes towards improvement that we have made to improve ESTHER during the past 8 years since our 2004 update. In particular, we generated 87 new families and increased the coverage of the UniProt Knowledgebase (UniProtKB). We also renewed the ESTHER website and added new visualization tools, such as the Overall Table and the Family Tree. We also address two topics of particular interest to the ESTHER users. First, we explain how the different enzyme classifications (bacterial lipases, peptidases, carboxylesterases) used by different communities of users are combined in ESTHER. Second, we discuss how variations of core architecture or in predicted active site residues result in a more precise clustering of families, and whether this strategy provides trustable hints to identify enzyme-like proteins with no catalytic activity. Oxford University Press 2013-01 2012-11-26 /pmc/articles/PMC3531081/ /pubmed/23193256 http://dx.doi.org/10.1093/nar/gks1154 Text en © The Author(s) 2012. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/3.0/), which permits non-commercial reuse, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com. |
spellingShingle | Articles Lenfant, Nicolas Hotelier, Thierry Velluet, Eric Bourne, Yves Marchot, Pascale Chatonnet, Arnaud ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions |
title | ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions |
title_full | ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions |
title_fullStr | ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions |
title_full_unstemmed | ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions |
title_short | ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions |
title_sort | esther, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3531081/ https://www.ncbi.nlm.nih.gov/pubmed/23193256 http://dx.doi.org/10.1093/nar/gks1154 |
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