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- W2042022353 abstract "Carbapenem-hydrolyzing class D β-lactamases (CHDLs) are enzymes found in important Gram-negative pathogens (mainly Acinetobacter baumannii and Enterobacteriaceae) that confer resistance to β-lactam antibiotics, and notably carbapenems. The crystal structure of the OXA-48 carbapenemase was determined at pH 7.5 and at a resolution of 1.9 Å. Surprisingly, and by contrast with OXA-24, the only other CHDL of known crystal structure, the structure of OXA-48 was similar to OXA-10, an enzyme devoid of carbapenemase activity, indicating that the hydrolysis of these compounds could depend on subtle changes in the active site region. Moreover, the active site groove of OXA-48 was different from that of OXA-24 in shape, dimensions, and charge distribution. Molecular dynamics pointed to the functional relevance of residues located in or close to the β5–β6 loop and allowed us to propose a mechanism for carbapenem hydrolysis by OXA-48." @default.
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- W2042022353 date "2009-05-01" @default.
- W2042022353 modified "2023-10-16" @default.
- W2042022353 title "Crystal Structure of the OXA-48 β-Lactamase Reveals Mechanistic Diversity among Class D Carbapenemases" @default.
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- W2042022353 doi "https://doi.org/10.1016/j.chembiol.2009.04.010" @default.
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