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The X‐ray crystal structure of the Acinetobacter‐Derived Cephalosporinase, ADC‐7, at 1.7 Å
Author(s) -
Porambo Alex,
Florek Nicholas,
Powers Rachel,
Wallar Brad
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.561.14
Subject(s) - cephalosporin , acinetobacter , acinetobacter baumannii , antibiotics , microbiology and biotechnology , antibiotic resistance , antimicrobial chemotherapy , antimicrobial , enzyme , crystal structure , bacteria , chemistry , biology , biochemistry , crystallography , genetics , pseudomonas aeruginosa
β‐Lactam resistance in Acinetobacter baumannii presents one of the greatest challenges to contemporary antimicrobial chemotherapy. The Acinetobacter ‐Derived Cephalosporinases (ADCs) are class C β ‐ lactamases found in A. baumannii and other Acinetobacter species that are responsible for resistance to penicillins, cephalosporins, and β‐lactam‐β‐lactamase inhibitor combinations. In order to probe the mechanism of substrate turnover, as well as to design novel β‐lactam antibiotics, it was important to elucidate the protein structure of an ADC enzyme. Here, we report the successful purification, crystallization, and determination of the crystal structure of ADC‐7 at 1.7 Å. This complete structure allows for the critical comparison of the overall structure and active site architecture of ADC‐7 with the known cephalosporinase, AmpC. Hopefully, our work will contribute to the development of a structure/function relationship for ADC‐7 that will provide insight into bacterial antibiotic resistance.