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Conformational Change Observed in the Active Site of Class C β-Lactamase MOX-1 upon Binding to Aztreonam
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...
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| Published in: | Antimicrob Agents Chemother |
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| Main Authors: | , , |
| Format: | Artigo |
| Language: | Inglês |
| Published: |
American Society for Microbiology
2015
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| Subjects: | |
| Online Access: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4505233/ https://ncbi.nlm.nih.gov/pubmed/26055361 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/AAC.04428-14 |
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