High adaptability of the omega loop underlies the substrate-spectrum-extension evolution of a class A β-lactamase, PenL
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/srep36527.pdf
Reference42 articles.
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2. Salverda, M. L., De Visser, J. A. & Barlow, M. Natural evolution of TEM-1 beta-lactamase: experimental reconstruction and clinical relevance. FEMS Microbiol Rev 34, 1015–1036 (2010).
3. Matagne, A., Lamotte-Brasseur, J. & Frere, J. Catalytic properties of class A β-lactamases: efficiency and diversity. Biochem. J 330, 581–598 (1998).
4. Yi, H. et al. Twelve Positions in a β-Lactamase That Can Expand Its Substrate Spectrum with a Single Amino Acid Substitution. PLoS ONE 7, e37585 (2012).
5. Fetrow, J. S. Omega loops: nonregular secondary structures significant in protein function and stability. The FASEB Journal 9, 708–717 (1995).
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