Investigating the effects of double mutation C30A/C75A on onconase structure: Studies at atomic resolution

ABSTRACT The structure of onconase C30A/C75A double mutant has been determined at 1.12Å 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 th...

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Published in:Biopolymers 2014-05, Vol.101 (5), p.454-460
Main Authors: Kurpiewska, Katarzyna, Torrent, Gerard, Ribó, Marc, Loch, Joanna I., Vilanova, Maria, Lewiński, Krzysztof
Format: Article
Language:English
Subjects:
Animals
atomic resolution
Catalytic Domain
Crystallography, X-Ray
double mutant onconase
Models, Molecular
Mutation - genetics
protein engineering
ranpirnase
Ribonucleases - chemistry
Static Electricity
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Summary:ABSTRACT The structure of onconase C30A/C75A double mutant has been determined at 1.12Å 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. © 2013 Wiley Periodicals, Inc. Biopolymers 101: 454–460, 2014.
ISSN:0006-3525
1097-0282
DOI:10.1002/bip.22403