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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Noguera, M. E. | es |
dc.contributor.author | Vázquez, D. S. | es |
dc.contributor.author | Ferrer-Sueta, Gerardo | es |
dc.contributor.author | Agudelo, W. A. | es |
dc.contributor.author | Howard, E. | es |
dc.contributor.author | Rasia, R. M. | es |
dc.contributor.author | Manta, Bruno | es |
dc.contributor.author | Cousido-Siah, A. | es |
dc.contributor.author | Mitschler, A. | es |
dc.contributor.author | Podjarny, A. | es |
dc.contributor.author | Santos, Javier | es |
dc.date.accessioned | 2019-10-02T22:08:26Z | - |
dc.date.available | 2019-10-02T22:08:26Z | - |
dc.date.issued | 2017 | es |
dc.date.submitted | 20190930 | es |
dc.identifier.citation | Noguera, M.E., et al. Structural variability of E. coli thioredoxin captured in the crystal structures of single-point mutants. Scientific Reports, 2017, 7, art. nro. 42343. doi: 10.1038/srep42343 | es |
dc.identifier.issn | 2045-2322 | es |
dc.identifier.uri | https://hdl.handle.net/20.500.12008/22013 | - |
dc.description.abstract | Thioredoxin is a ubiquitous small protein that catalyzes redox reactions of protein thiols. Additionally, thioredoxin from E. coli (EcTRX) is a widely-used model for structure-function studies. In a previous paper, we characterized several single-point mutants of the C-terminal helix (CTH) that alter global stability of EcTRX. However, spectroscopic signatures and enzymatic activity for some of these mutants were found essentially unaffected. A comprehensive structural characterization at the atomic level of these near-invariant mutants can provide detailed information about structural variability of EcTRX. We address this point through the determination of the crystal structures of four point-mutants, whose mutations occurs within or near the CTH, namely L94A, E101G, N106A and L107A. These structures are mostly unaffected compared with the wild-type variant. Notably, the E101G mutant presents a large region with two alternative traces for the backbone of the same chain. It represents a significant shift in backbone positions. Enzymatic activity measurements and conformational dynamics studies monitored by NMR and molecular dynamic simulations show that E101G mutation results in a small effect in the structural features of the protein. We hypothesize that these alternative conformations represent samples of the native-state ensemble of EcTRX, specifically the magnitude and location of conformational heterogeneity. | es |
dc.format.mimetype | application/pdf | es |
dc.language.iso | en | es |
dc.publisher | Nature Publishing Group | es |
dc.relation.ispartof | Scientific Reports, 2017, 7, art. no. 42343 | es |
dc.rights | 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) | es |
dc.subject | Cysteine | es |
dc.subject | Mutant protein | es |
dc.subject | Thioredoxin | es |
dc.subject | Alkylation | es |
dc.subject | Chemistry | es |
dc.subject | Escherichia coli | es |
dc.subject | Genetics | es |
dc.subject | Metabolism | es |
dc.subject | Molecular dynamics | es |
dc.title | Structural variability of E. coli thioredoxin captured in the crystal structures of single-point mutants | es |
dc.type | Artículo | es |
dc.contributor.filiacion | Ferrer-Sueta, Gerardo. Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Química Biológica | es |
dc.contributor.filiacion | Manta, Bruno. Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Química Biológica | es |
dc.rights.licence | Licencia Creative Commons Atribución (CC –BY 4.0) | es |
dc.identifier.doi | 10.1038/srep42343 | es |
Aparece en las colecciones: | Publicaciones académicas y científicas - Facultad de Ciencias |
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101038srep42343.pdf | 1,59 MB | Adobe PDF | Visualizar/Abrir |
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