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Investigating the Effects of Double Mutation C30A/C75A on Onconase Structure: Studies at Atomic Resolution

The structure of onconase C30A/C75A double mutant has been determined at 1.12A° resolution. The structure has high structural homology to other onconase structures. The changes being results of mutation are relatively small, distributed asymmetrically around the two mutated positions, and they are observed not only in the mutation region but expanded to entire molecule. Different conformation of Lys31 side chain that influences the hydrogen bonding network around catalytic triad is probably responsible for lower catalytic efficiency of double mutant. The decrease in thermal stability observed for the onconase variant might be explained by a less dense packing as manifested by the increase of the molecular volume and the solvent accessible surface area

Wiley

Director: Ministerio de Ciencia e Innovación (Espanya)
Autor: Kurpiewska, Katarzyna
Torrent Alberti, Gerard
Ribó i Panosa, Marc
Loch, Joanna I.
Vilanova i Brugués, Maria
Lewiński, Krzysztof
Data: 2014
Resum: The structure of onconase C30A/C75A double mutant has been determined at 1.12A° resolution. The structure has high structural homology to other onconase structures. The changes being results of mutation are relatively small, distributed asymmetrically around the two mutated positions, and they are observed not only in the mutation region but expanded to entire molecule. Different conformation of Lys31 side chain that influences the hydrogen bonding network around catalytic triad is probably responsible for lower catalytic efficiency of double mutant. The decrease in thermal stability observed for the onconase variant might be explained by a less dense packing as manifested by the increase of the molecular volume and the solvent accessible surface area
Format: application/pdf
Accés al document: http://hdl.handle.net/10256/12103
Llenguatge: eng
Editor: Wiley
Col·lecció: info:eu-repo/semantics/altIdentifier/doi/10.1002/bip.22403
info:eu-repo/semantics/altIdentifier/issn/0006-3525
info:eu-repo/semantics/altIdentifier/eissn/1097-0282
info:eu-repo/grantAgreement/MICINN//BFU2009-06935/ES/Bases Moleculares Del Plegamiento Y Citotoxicidad De Las Ribonucleasas Pancreaticas. Evaluacion De La Actividad Citotoxica Y Diseño De Estrategias Para Su Control Mediante Splicing Proteico./
Drets: Tots els drets reservats
Matèria: Ribonucleases
Enzims
Enzymes
Enginyeria de proteïnes
Protein engineering
Títol: Investigating the Effects of Double Mutation C30A/C75A on Onconase Structure: Studies at Atomic Resolution
Tipus: info:eu-repo/semantics/article
Repositori: DUGiDocs

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