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Published on: March 25, 2017
Conformational Change Observed in the Active Site of Class C β-Lactamase MOX-1 upon Binding to Aztreonam
Takuma Oguri1, Yoshikazu Ishii2, Akiko Shimizu-Ibuka3
1Department of Science, Yamagata University, Yamagata, Japan.
Abstract:
We solved the crystal structure of the class C β-lactamase MOX-1 complexed with the inhibitor aztreonam at 1.9Å resolution. The main-chain oxygen of Ser315 interacts with the amide nitrogen of aztreonam. Surprisingly, compared to that in the structure of free MOX-1, this main-chain carboxyl changes its position significantly upon binding to aztreonam. This result indicates that the interaction between MOX-1 and β-lactams can be accompanied by conformational changes in the B3 β-strand main chain.
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