Alternative Model for RND-Type Efflux Pump
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Outros Autores: | , , |
Tipo de documento: | Relatório |
Idioma: | eng |
Título da fonte: | Journal of the Brazilian Chemical Society (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532016001202383 |
Resumo: | RND (resistance-nodulation-division) transporters are found in several Gram-negative bacteria species. These proteins form a complex along with membrane fusion proteins and outer membrane factors. This complex acts as an efflux pump, transporting several different molecules directly from the cytoplasm to the extracellular medium. Although the crystallographic structure of each protein of the complex is known, the complete complex assembly is not yet fully characterized. In 2014, a model for the complete system, based upon a cryoelectron-microscopy map, was proposed. In the present work, we propose an alternative model that also satisfies the volume obtained from the cryoelectron-microscopy assay. In this model, the AcrA helical domains are interleaved to the helical domains of the TolC protein, increasing the diameter of the formed pore. We believe that this model represents a better model for RND-type efflux pump and might contribute to the characterization of this system. |
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Alternative Model for RND-Type Efflux PumpRND efflux systemcomparative modelingefflux pumpmolecular modelingprotein structureRND (resistance-nodulation-division) transporters are found in several Gram-negative bacteria species. These proteins form a complex along with membrane fusion proteins and outer membrane factors. This complex acts as an efflux pump, transporting several different molecules directly from the cytoplasm to the extracellular medium. Although the crystallographic structure of each protein of the complex is known, the complete complex assembly is not yet fully characterized. In 2014, a model for the complete system, based upon a cryoelectron-microscopy map, was proposed. In the present work, we propose an alternative model that also satisfies the volume obtained from the cryoelectron-microscopy assay. In this model, the AcrA helical domains are interleaved to the helical domains of the TolC protein, increasing the diameter of the formed pore. We believe that this model represents a better model for RND-type efflux pump and might contribute to the characterization of this system.Sociedade Brasileira de Química2016-12-01info:eu-repo/semantics/reportinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532016001202383Journal of the Brazilian Chemical Society v.27 n.12 2016reponame:Journal of the Brazilian Chemical Society (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.5935/0103-5053.20160125info:eu-repo/semantics/openAccessTorres,Pedro Henrique MonteiroPascutti,Pedro GeraldoBisch,Paulo MascarelloSilva,Manuela Leal daeng2016-12-01T00:00:00Zoai:scielo:S0103-50532016001202383Revistahttp://jbcs.sbq.org.brONGhttps://old.scielo.br/oai/scielo-oai.php||office@jbcs.sbq.org.br1678-47900103-5053opendoar:2016-12-01T00:00Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)false |
dc.title.none.fl_str_mv |
Alternative Model for RND-Type Efflux Pump |
title |
Alternative Model for RND-Type Efflux Pump |
spellingShingle |
Alternative Model for RND-Type Efflux Pump Torres,Pedro Henrique Monteiro RND efflux system comparative modeling efflux pump molecular modeling protein structure |
title_short |
Alternative Model for RND-Type Efflux Pump |
title_full |
Alternative Model for RND-Type Efflux Pump |
title_fullStr |
Alternative Model for RND-Type Efflux Pump |
title_full_unstemmed |
Alternative Model for RND-Type Efflux Pump |
title_sort |
Alternative Model for RND-Type Efflux Pump |
author |
Torres,Pedro Henrique Monteiro |
author_facet |
Torres,Pedro Henrique Monteiro Pascutti,Pedro Geraldo Bisch,Paulo Mascarello Silva,Manuela Leal da |
author_role |
author |
author2 |
Pascutti,Pedro Geraldo Bisch,Paulo Mascarello Silva,Manuela Leal da |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Torres,Pedro Henrique Monteiro Pascutti,Pedro Geraldo Bisch,Paulo Mascarello Silva,Manuela Leal da |
dc.subject.por.fl_str_mv |
RND efflux system comparative modeling efflux pump molecular modeling protein structure |
topic |
RND efflux system comparative modeling efflux pump molecular modeling protein structure |
description |
RND (resistance-nodulation-division) transporters are found in several Gram-negative bacteria species. These proteins form a complex along with membrane fusion proteins and outer membrane factors. This complex acts as an efflux pump, transporting several different molecules directly from the cytoplasm to the extracellular medium. Although the crystallographic structure of each protein of the complex is known, the complete complex assembly is not yet fully characterized. In 2014, a model for the complete system, based upon a cryoelectron-microscopy map, was proposed. In the present work, we propose an alternative model that also satisfies the volume obtained from the cryoelectron-microscopy assay. In this model, the AcrA helical domains are interleaved to the helical domains of the TolC protein, increasing the diameter of the formed pore. We believe that this model represents a better model for RND-type efflux pump and might contribute to the characterization of this system. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016-12-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/report |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
report |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532016001202383 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532016001202383 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.5935/0103-5053.20160125 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
dc.source.none.fl_str_mv |
Journal of the Brazilian Chemical Society v.27 n.12 2016 reponame:Journal of the Brazilian Chemical Society (Online) instname:Sociedade Brasileira de Química (SBQ) instacron:SBQ |
instname_str |
Sociedade Brasileira de Química (SBQ) |
instacron_str |
SBQ |
institution |
SBQ |
reponame_str |
Journal of the Brazilian Chemical Society (Online) |
collection |
Journal of the Brazilian Chemical Society (Online) |
repository.name.fl_str_mv |
Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ) |
repository.mail.fl_str_mv |
||office@jbcs.sbq.org.br |
_version_ |
1750318179114024960 |