Substrate recognition properties from an intermediate structural state of the UreA transporter

Through a combination of comparative modeling, site-directed and classical random mutagenesis approaches, we previously identified critical residues for binding, recognition, and translocation of urea, and its inhibition by 2-thiourea and acetamide in the Aspergillus nidulans urea transporter, UreA....

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Main Author: Sanguinetti Miralles, Manuel (author)
Other Authors: Silva Santos, Lucianna Helene (author), Dourron, Juliette (author), Alamón Lima, Catalina Isadora (author), Idiarte Montiel, Juan (author), Amillis, Sotiris (author), Pantano, Sergio (author), Ramón, Ana (author)
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Language:English
Published: 2022
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Online Access:https://hdl.handle.net/20.500.12008/41370
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author Sanguinetti Miralles, Manuel
author2 Silva Santos, Lucianna Helene
Dourron, Juliette
Alamón Lima, Catalina Isadora
Idiarte Montiel, Juan
Amillis, Sotiris
Pantano, Sergio
Ramón, Ana
author2_role author
author
author
author
author
author
author
author_browse Alamón Lima, Catalina Isadora
Amillis, Sotiris
Dourron, Juliette
Idiarte Montiel, Juan
Pantano, Sergio
Ramón, Ana
Sanguinetti Miralles, Manuel
Silva Santos, Lucianna Helene
author_facet Sanguinetti Miralles, Manuel
Silva Santos, Lucianna Helene
Dourron, Juliette
Alamón Lima, Catalina Isadora
Idiarte Montiel, Juan
Amillis, Sotiris
Pantano, Sergio
Ramón, Ana
author_role author
collection COLIBRI
dc.contributor.none.fl_str_mv Sanguinetti Miralles Manuel, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.
Silva Santos Lucianna Helene, Instituto Pasteur (Montevideo).
Dourron Juliette, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.
Alamón Lima Catalina Isadora, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.
Idiarte Montiel Juan, Instituto Pasteur (Montevideo).
Amillis Sotiris
Pantano Sergio, Instituto Pasteur (Montevideo).
Ramón Ana, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.
dc.creator.none.fl_str_mv Sanguinetti Miralles, Manuel
Silva Santos, Lucianna Helene
Dourron, Juliette
Alamón Lima, Catalina Isadora
Idiarte Montiel, Juan
Amillis, Sotiris
Pantano, Sergio
Ramón, Ana
dc.date.none.fl_str_mv 2022
2023-11-21T12:01:21Z
2023-11-21T12:01:21Z
dc.format.none.fl_str_mv 17 h.
application/pdf
dc.identifier.none.fl_str_mv Sanguinetti Miralles, M, Silva Santos, L, Dourron, J, [y otros autores]. "Substrate recognition properties from an intermediate structural state of the UreA transporter". International Journal of Molecular Science. [en línea] 2022, 23(24): 16039. 17 h. DOI: 10.3390/ijms232416039
1422-0067
https://hdl.handle.net/20.500.12008/41370
10.3390/ijms232416039
dc.language.none.fl_str_mv en_US
eng
dc.publisher.none.fl_str_mv MDPI
dc.relation.none.fl_str_mv International Journal of Molecular Science, 2022, 23(24): 16039.
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
Licencia Creative Commons Atribución (CC - By 4.0)
dc.source.none.fl_str_mv reponame:COLIBRI
instname:Universidad de la República
instacron:Universidad de la República
dc.subject.none.fl_str_mv Aspergillus nidulans
Urea transport
AlphaFold2
Binding site
Molecular docking
dc.title.none.fl_str_mv Substrate recognition properties from an intermediate structural state of the UreA transporter
dc.type.none.fl_str_mv Artículo
info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
description Through a combination of comparative modeling, site-directed and classical random mutagenesis approaches, we previously identified critical residues for binding, recognition, and translocation of urea, and its inhibition by 2-thiourea and acetamide in the Aspergillus nidulans urea transporter, UreA. To deepen the structural characterization of UreA, we employed the artificial intelligence (AI) based AlphaFold2 (AF2) program. In this analysis, the resulting AF2 models lacked inward- and outward-facing cavities, suggesting a structural intermediate state of UreA. Moreover, the orientation of the W82, W84, N279, and T282 side chains showed a large variability, which in the case of W82 and W84, may operate as a gating mechanism in the ligand pathway. To test this hypothesis non-conservative and conservative substitutions of these amino acids were introduced, and binding and transport assessed for urea and its toxic analogue 2-thiourea, as well as binding of the structural analogue acetamide. As a result, residues W82, W84, N279, and T282 were implicated in substrate identification, selection, and translocation. Using molecular docking with Autodock Vina with flexible side chains, we corroborated the AF2 theoretical intermediate model, showing a remarkable correlation between docking scores and experimental affinities determined in wild-type and UreA mutants. The combination of AI-based modeling with classical docking, validated by comprehensive mutational analysis at the binding region, would suggest an unforeseen option to determine structural level details on a challenging family of proteins.
eu_rights_str_mv openAccess
format article
id anni_434550b599cdfee5d35b83e8c1941c4e
identifier_str_mv Sanguinetti Miralles, M, Silva Santos, L, Dourron, J, [y otros autores]. "Substrate recognition properties from an intermediate structural state of the UreA transporter". International Journal of Molecular Science. [en línea] 2022, 23(24): 16039. 17 h. DOI: 10.3390/ijms232416039
1422-0067
10.3390/ijms232416039
instacron_str Universidad de la República
institution Universidad de la República
instname_str Universidad de la República
language eng
language_invalid_str_mv en_US
network_acronym_str anni
network_name_str oai-lr-anni
oai_identifier_str oai:colibri.udelar.edu.uy:20.500.12008/41370
publishDate 2022
publishDateSort 2022
publisher.none.fl_str_mv MDPI
reponame_str COLIBRI
repository.mail.fl_str_mv
repository.name.fl_str_mv
repository_id_str
rights_invalid_str_mv Licencia Creative Commons Atribución (CC - By 4.0)
spelling Substrate recognition properties from an intermediate structural state of the UreA transporterSanguinetti Miralles, ManuelSilva Santos, Lucianna HeleneDourron, JulietteAlamón Lima, Catalina IsadoraIdiarte Montiel, JuanAmillis, SotirisPantano, SergioRamón, AnaAspergillus nidulansUrea transportAlphaFold2Binding siteMolecular dockingThrough a combination of comparative modeling, site-directed and classical random mutagenesis approaches, we previously identified critical residues for binding, recognition, and translocation of urea, and its inhibition by 2-thiourea and acetamide in the Aspergillus nidulans urea transporter, UreA. To deepen the structural characterization of UreA, we employed the artificial intelligence (AI) based AlphaFold2 (AF2) program. In this analysis, the resulting AF2 models lacked inward- and outward-facing cavities, suggesting a structural intermediate state of UreA. Moreover, the orientation of the W82, W84, N279, and T282 side chains showed a large variability, which in the case of W82 and W84, may operate as a gating mechanism in the ligand pathway. To test this hypothesis non-conservative and conservative substitutions of these amino acids were introduced, and binding and transport assessed for urea and its toxic analogue 2-thiourea, as well as binding of the structural analogue acetamide. As a result, residues W82, W84, N279, and T282 were implicated in substrate identification, selection, and translocation. Using molecular docking with Autodock Vina with flexible side chains, we corroborated the AF2 theoretical intermediate model, showing a remarkable correlation between docking scores and experimental affinities determined in wild-type and UreA mutants. The combination of AI-based modeling with classical docking, validated by comprehensive mutational analysis at the binding region, would suggest an unforeseen option to determine structural level details on a challenging family of proteins.ANII: FCE_3_2018_1_148002MDPISanguinetti Miralles Manuel, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.Silva Santos Lucianna Helene, Instituto Pasteur (Montevideo).Dourron Juliette, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.Alamón Lima Catalina Isadora, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.Idiarte Montiel Juan, Instituto Pasteur (Montevideo).Amillis SotirisPantano Sergio, Instituto Pasteur (Montevideo).Ramón Ana, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.2023-11-21T12:01:21Z2023-11-21T12:01:21Z2022Artículoinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion17 h.application/pdfSanguinetti Miralles, M, Silva Santos, L, Dourron, J, [y otros autores]. "Substrate recognition properties from an intermediate structural state of the UreA transporter". International Journal of Molecular Science. [en línea] 2022, 23(24): 16039. 17 h. DOI: 10.3390/ijms2324160391422-0067https://hdl.handle.net/20.500.12008/4137010.3390/ijms232416039reponame:COLIBRIinstname:Universidad de la Repúblicainstacron:Universidad de la Repúblicaen_USengInternational Journal of Molecular Science, 2022, 23(24): 16039.Las obras depositadas en el Repositorio se rigen por la Ordenanza de los Derechos de la Propiedad Intelectual de la Universidad de la República.(Res. Nº 91 de C.D.C. de 8/III/1994 – D.O. 7/IV/1994) y por la Ordenanza del Repositorio Abierto de la Universidad de la República (Res. Nº 16 de C.D.C. de 07/10/2014)info:eu-repo/semantics/openAccessLicencia Creative Commons Atribución (CC - By 4.0)oai:colibri.udelar.edu.uy:20.500.12008/413702026-04-14T10:10:21Z
spellingShingle Substrate recognition properties from an intermediate structural state of the UreA transporter
Sanguinetti Miralles, Manuel
Aspergillus nidulans
Urea transport
AlphaFold2
Binding site
Molecular docking
status_str publishedVersion
title Substrate recognition properties from an intermediate structural state of the UreA transporter
title_full Substrate recognition properties from an intermediate structural state of the UreA transporter
title_fullStr Substrate recognition properties from an intermediate structural state of the UreA transporter
title_full_unstemmed Substrate recognition properties from an intermediate structural state of the UreA transporter
title_short Substrate recognition properties from an intermediate structural state of the UreA transporter
title_sort Substrate recognition properties from an intermediate structural state of the UreA transporter
topic Aspergillus nidulans
Urea transport
AlphaFold2
Binding site
Molecular docking
url https://hdl.handle.net/20.500.12008/41370