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ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions

Authors :
Eric Velluet
Nicolas Lenfant
Thierry Hotelier
Yves Bourne
Arnaud Chatonnet
Pascale Marchot
Différenciation Cellulaire et Croissance (DCC)
Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Recherche Agronomique (INRA)
Architecture et fonction des macromolécules biologiques (AFMB)
Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)
SDAR Occitanie Montpellier (SDAR)
Institut National de la Recherche Agronomique (INRA)
Chatonnet, Arnaud
Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2)
Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA)
Dynamique Musculaire et Métabolisme (DMEM)
Institut National de la Recherche Agronomique (INRA)-Université de Montpellier (UM)
Source :
Nucleic Acids Research, Nucleic Acids Research, Oxford University Press, 2013, 41, pp.423-429. ⟨10.1093/nar/gks1154⟩, Nucleic Acids Research (41), 423–429. (2013), Nucleic Acids Research, 2013, 41, pp.423-429. ⟨10.1093/nar/gks1154⟩
Publication Year :
2013
Publisher :
HAL CCSD, 2013.

Abstract

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.

Details

Language :
English
ISSN :
03051048 and 13624962
Database :
OpenAIRE
Journal :
Nucleic Acids Research, Nucleic Acids Research, Oxford University Press, 2013, 41, pp.423-429. ⟨10.1093/nar/gks1154⟩, Nucleic Acids Research (41), 423–429. (2013), Nucleic Acids Research, 2013, 41, pp.423-429. ⟨10.1093/nar/gks1154⟩
Accession number :
edsair.doi.dedup.....c50dc71d1c5a14cf2b68fcea1483e536
Full Text :
https://doi.org/10.1093/nar/gks1154⟩