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 o...
| Authors: | , , , , , |
|---|---|
| Format: | article |
| Status: | Published version |
| Publication Date: | 2014 |
| Country: | España |
| Institution: | Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya) |
| Repository: | Recercat. Dipósit de la Recerca de Catalunya |
| OAI Identifier: | oai:recercat.cat:10256/12103 |
| Online Access: | http://hdl.handle.net/10256/12103 |
| Access Level: | Embargoed access |
| Keyword: | Ribonucleases Enzims Enzymes Enginyeria de proteïnes Protein engineering |
| Summary: | 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 |
|---|