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Investigating the effects of double mutation C30A/C75A on onconase structure: Studies at atomic resolution
Author(s) -
Kurpiewska Katarzyna,
Torrent Gerard,
Ribó Marc,
Loch Joanna I.,
Vilanova Maria,
Lewiński Krzysztof
Publication year - 2014
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22403
Subject(s) - chemistry , mutant , catalysis , molecule , thermal stability , mutation , catalytic efficiency , hydrogen bond , crystallography , stereochemistry , biophysics , biochemistry , organic chemistry , gene , biology
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.