Structural highlights
Publication Abstract from PubMed
We solved the crystal structure of a class C beta-lactamase MOX-1 complexed with an inhibitor, aztreonam, at 1.9A resolution. The main-chain oxygen of Ser315 interacts with the amide nitrogen of aztreonam. Surprisingly, compared to the free MOX-1 structure, this main-chain carboxyl changes its position significantly upon binding aztreonam. This result indicates that the interaction between MOX-1 and beta-lactams can be accompanied by conformational changes of the B3 beta-strand main chain.
A Conformational Change Observed in the Active Site of Class C beta-Lactamase MOX-1 in Binding Aztreonam.,Oguri T, Ishii Y, Shimizu-Ibuka A Antimicrob Agents Chemother. 2015 Jun 8. pii: AAC.04428-14. PMID:26055361[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Oguri T, Ishii Y, Shimizu-Ibuka A. A Conformational Change Observed in the Active Site of Class C beta-Lactamase MOX-1 in Binding Aztreonam. Antimicrob Agents Chemother. 2015 Jun 8. pii: AAC.04428-14. PMID:26055361 doi:http://dx.doi.org/10.1128/AAC.04428-14
