1.8 Å resolution crystal structure of the carbapenem intrinsic resistance protein CarF
Acta Crystallographica Section D: Biological Crystallography
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Tichy, E., Hardwick, S., Luisi, B., & Salmond, G. (2017). 1.8 Å resolution crystal structure of the carbapenem intrinsic resistance protein CarF. Acta Crystallographica Section D: Biological Crystallography, 73 (7), 549-556. https://doi.org/10.1107/S2059798317002236
The natural production of the beta-lactam antibiotic carbapenem in bacteria involves a group of enzymes that form a synthetic pathway as well as proteins that protect the cell from self-intoxification by the products. We report the crystal structure of CarF, one of the two proteins that confers resistance to the antibiotic synthesis in the host organism. The CarF fold places it within a widely occurring structural family, indicating an ancient structural origin from which the resistance function has been derived.
antibiotic resistance, carbapenem, intrinsic resistance, CIR family, CLec domain
This work was supported by a Herchel Smith PhD scholarship to Evelyn Tichy. Ben Luisi is supported by the Wellcome Trust and work in the Salmond laboratory is supported by the Biotechnology and Biological Sciences Research Council, UK.
WELLCOME TRUST (200873/Z/16/Z)
Wellcome Trust (076846/Z/05/B)
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External DOI: https://doi.org/10.1107/S2059798317002236
This record's URL: https://www.repository.cam.ac.uk/handle/1810/263955