Conformational Change Observed in the Active Site of Class C β-Lactamase MOX-1 upon Binding to Aztreonam | Zendy

Takuma Oguri | Zendy; Yoshikazu Ishii | Zendy; Akiko ShimizuIbuka | Zendy

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Conformational Change Observed in the Active Site of Class C β-Lactamase MOX-1 upon Binding to Aztreonam

Author(s) -

Takuma Oguri,

Yoshikazu Ishii,

Akiko ShimizuIbuka

Publication year - 2015

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.04428-14

Subject(s) - aztreonam , chemistry , conformational change , amide , mox fuel , stereochemistry , active site , binding site , crystal structure , crystallography , biochemistry , enzyme , antibiotics , radiochemistry , antibiotic resistance , imipenem , plutonium

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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