Event Title

The X-ray Crystal Structure of the Acinetobacter-Derived Cephalosporinase, ADC-7, at 1.7 Ã…

Presentation Type

Poster/Portfolio

Presenter Major(s)

Cell and Molecular Biology

Mentor Information

Brad Wallar

Department

Chemistry

Location

Kirkhof Center KC 83

Start Date

10-4-2013 11:00 AM

End Date

10-4-2013 12:00 PM

Keywords

Health

Abstract

Beta-lactam resistance in Acinetobacter baumannii presents one of the challenges to current antimicrobial chemotherapy. The Acinetobacter-Derived Cephalosporinases (ADCs) are class C beta-lactamases found in A. baumannii and other Acinetobacter species that are responsible for resistance to penicillins, cephalosporins, and beta-lactam-beta-lactamase inhibitor combinations. In order to probe the mechanism of substrate turnover, as well as to design novel beta-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 Ã…. This 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.

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Apr 10th, 11:00 AM Apr 10th, 12:00 PM

The X-ray Crystal Structure of the Acinetobacter-Derived Cephalosporinase, ADC-7, at 1.7 Ã…

Kirkhof Center KC 83

Beta-lactam resistance in Acinetobacter baumannii presents one of the challenges to current antimicrobial chemotherapy. The Acinetobacter-Derived Cephalosporinases (ADCs) are class C beta-lactamases found in A. baumannii and other Acinetobacter species that are responsible for resistance to penicillins, cephalosporins, and beta-lactam-beta-lactamase inhibitor combinations. In order to probe the mechanism of substrate turnover, as well as to design novel beta-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 Ã…. This 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.