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Literature DB >> 26055361

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.

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.

Entities: Chemical Gene

Mesh：

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Year: 2015 PMID： 26055361 PMCID： PMC4505233 DOI： 10.1128/AAC.04428-14

Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN： 0066-4804 Impact factor: 5.191

14 in total

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3 in total