DataSheet1_Structural and evolutionary insights into astacin metallopeptidases.DOCX [Dataset]

The astacins are a family of metallopeptidases (MPs) that has been extensively described from animals. They are multidomain extracellular proteins, which have a conserved core architecture encompassing a signal peptide for secretion, a prodomain or prosegment and a zinc-dependent catalytic domain (C...

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Detalles Bibliográficos
Autores: Gomis-Rüth, F. Xavier, Stöcker, Walter
Tipo de recurso: conjunto de datos
Estado:Versión publicada
Fecha de publicación:2023
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/359624
Acceso en línea:http://hdl.handle.net/10261/359624
Access Level:acceso abierto
Palabra clave:Evolution of metallopeptidases
Catalytic domain (CD)
Darwinian descent
Horizontal gene transfer (HGT)
Phylogeny of enzymes
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spelling DataSheet1_Structural and evolutionary insights into astacin metallopeptidases.DOCX [Dataset]Gomis-Rüth, F. XavierStöcker, WalterEvolution of metallopeptidasesCatalytic domain (CD)Darwinian descentHorizontal gene transfer (HGT)Phylogeny of enzymesThe astacins are a family of metallopeptidases (MPs) that has been extensively described from animals. They are multidomain extracellular proteins, which have a conserved core architecture encompassing a signal peptide for secretion, a prodomain or prosegment and a zinc-dependent catalytic domain (CD). This constellation is found in the archetypal name-giving digestive enzyme astacin from the European crayfish Astacus astacus. Astacin catalytic domains span ∼200 residues and consist of two subdomains that flank an extended active-site cleft. They share several structural elements including a long zinc-binding consensus sequence (HEXXHXXGXXH) immediately followed by an EXXRXDRD motif, which features a family-specific glutamate. In addition, a downstream SIMHY-motif encompasses a “Met-turn” methionine and a zinc-binding tyrosine. The overall architecture and some structural features of astacin catalytic domains match those of other more distantly related MPs, which together constitute the metzincin clan of metallopeptidases. We further analysed the structures of PRO-, MAM, TRAF, CUB and EGF-like domains, and described their essential molecular determinants. In addition, we investigated the distribution of astacins across kingdoms and their phylogenetic origin. Through extensive sequence searches we found astacin CDs in > 25,000 sequences down the tree of life from humans beyond Metazoa, including Choanoflagellata, Filasterea and Ichtyosporea. We also found < 400 sequences scattered across non-holozoan eukaryotes including some fungi and one virus, as well as in selected taxa of archaea and bacteria that are pathogens or colonizers of animal hosts, but not in plants. Overall, we propose that astacins originate in the root of Holozoa consistent with Darwinian descent and that the latter genes might be the result of horizontal gene transfer from holozoan donors.Peer reviewedFigshareConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202420242023info:eu-repo/semantics/datasethttp://purl.org/coar/resource_type/c_ddb1Publisher's versioninfo:eu-repo/semantics/publishedVersionapplication/mswordhttp://hdl.handle.net/10261/359624reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)InglésGomis-Rüth, F. Xavier; Stöcker, Walter. Structural and evolutionary insights into astacin metallopeptidases. http://dx.doi.org/10.3389/fmolb.2022.1080836 . http://hdl.handle.net/10261/335597https://doi.org/10.3389/fmolb.2022.1080836.s001Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3596242026-05-22T06:33:51Z
dc.title.none.fl_str_mv DataSheet1_Structural and evolutionary insights into astacin metallopeptidases.DOCX [Dataset]
title DataSheet1_Structural and evolutionary insights into astacin metallopeptidases.DOCX [Dataset]
spellingShingle DataSheet1_Structural and evolutionary insights into astacin metallopeptidases.DOCX [Dataset]
Gomis-Rüth, F. Xavier
Evolution of metallopeptidases
Catalytic domain (CD)
Darwinian descent
Horizontal gene transfer (HGT)
Phylogeny of enzymes
title_short DataSheet1_Structural and evolutionary insights into astacin metallopeptidases.DOCX [Dataset]
title_full DataSheet1_Structural and evolutionary insights into astacin metallopeptidases.DOCX [Dataset]
title_fullStr DataSheet1_Structural and evolutionary insights into astacin metallopeptidases.DOCX [Dataset]
title_full_unstemmed DataSheet1_Structural and evolutionary insights into astacin metallopeptidases.DOCX [Dataset]
title_sort DataSheet1_Structural and evolutionary insights into astacin metallopeptidases.DOCX [Dataset]
dc.creator.none.fl_str_mv Gomis-Rüth, F. Xavier
Stöcker, Walter
author Gomis-Rüth, F. Xavier
author_facet Gomis-Rüth, F. Xavier
Stöcker, Walter
author_role author
author2 Stöcker, Walter
author2_role author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Evolution of metallopeptidases
Catalytic domain (CD)
Darwinian descent
Horizontal gene transfer (HGT)
Phylogeny of enzymes
topic Evolution of metallopeptidases
Catalytic domain (CD)
Darwinian descent
Horizontal gene transfer (HGT)
Phylogeny of enzymes
description The astacins are a family of metallopeptidases (MPs) that has been extensively described from animals. They are multidomain extracellular proteins, which have a conserved core architecture encompassing a signal peptide for secretion, a prodomain or prosegment and a zinc-dependent catalytic domain (CD). This constellation is found in the archetypal name-giving digestive enzyme astacin from the European crayfish Astacus astacus. Astacin catalytic domains span ∼200 residues and consist of two subdomains that flank an extended active-site cleft. They share several structural elements including a long zinc-binding consensus sequence (HEXXHXXGXXH) immediately followed by an EXXRXDRD motif, which features a family-specific glutamate. In addition, a downstream SIMHY-motif encompasses a “Met-turn” methionine and a zinc-binding tyrosine. The overall architecture and some structural features of astacin catalytic domains match those of other more distantly related MPs, which together constitute the metzincin clan of metallopeptidases. We further analysed the structures of PRO-, MAM, TRAF, CUB and EGF-like domains, and described their essential molecular determinants. In addition, we investigated the distribution of astacins across kingdoms and their phylogenetic origin. Through extensive sequence searches we found astacin CDs in > 25,000 sequences down the tree of life from humans beyond Metazoa, including Choanoflagellata, Filasterea and Ichtyosporea. We also found < 400 sequences scattered across non-holozoan eukaryotes including some fungi and one virus, as well as in selected taxa of archaea and bacteria that are pathogens or colonizers of animal hosts, but not in plants. Overall, we propose that astacins originate in the root of Holozoa consistent with Darwinian descent and that the latter genes might be the result of horizontal gene transfer from holozoan donors.
publishDate 2023
dc.date.none.fl_str_mv 2023
2024
2024
dc.type.none.fl_str_mv info:eu-repo/semantics/dataset
http://purl.org/coar/resource_type/c_ddb1
Publisher's version
info:eu-repo/semantics/publishedVersion
format dataset
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/359624
url http://hdl.handle.net/10261/359624
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Gomis-Rüth, F. Xavier; Stöcker, Walter. Structural and evolutionary insights into astacin metallopeptidases. http://dx.doi.org/10.3389/fmolb.2022.1080836 . http://hdl.handle.net/10261/335597
https://doi.org/10.3389/fmolb.2022.1080836.s001
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/msword
dc.publisher.none.fl_str_mv Figshare
publisher.none.fl_str_mv Figshare
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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