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Título: | Conserved asparagine residue 54 of α-sarcin plays a role in protein stability and enzyme activity |
Autor: | Siemer, Ansgar; Masip, Manuel; Carreras, Nelson; García-Ortega, Lucía; Oñaderra, Mercedes; Bruix, M. CSIC ORCID ; Martínez-del-Pozo, Álvaro; Gavilanes, José G. | Palabras clave: | a-sarcin Protein stability Ribonuclease RNase T1 |
Fecha de publicación: | dic-2004 | Editor: | Walter de Gruyter | Citación: | Biological Chemistry 385: 1165-1170 (2004) | Resumen: | Asparagine 54 of a-sarcin is a conserved residue within the proteins of the ribotoxin family of microbial ribonucleases. It is located in loop 2 of the protein, which lacks repetitive secondary structure elements but exhibits a well-defined conformation. Five mutant variants at this residue have been produced and characterized. The spectroscopic characterization of these proteins indicates that the overall conformation is not changed upon mutation. Activity and denaturation assays show that Asn-54 largely contributes to protein stability, and its presence is a requirement for the highly specific inhibitory activity of these ribotoxins on ribosomes. | Versión del editor: | http://dx.doi.org/10.1515/BC.2004.150 | URI: | http://hdl.handle.net/10261/257810 | DOI: | 10.1515/BC.2004.150 | Identificadores: | doi: 10.1515/BC.2004.150 issn: 1431-6730 e-issn: 1437-4315 |
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accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
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