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Investigating protein structural plasticity by surveying the consequence of an amino acid deletion from TEM-1 β-lactamase

Simm, Alan M., Baldwin, Amy Joy, Busse, Kathy and Jones, D. Dafydd 2007. Investigating protein structural plasticity by surveying the consequence of an amino acid deletion from TEM-1 β-lactamase. FEBS Letters 581 (21) , pp. 3904-3908. 10.1016/j.febslet.2007.07.018

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Abstract

While the deletion of an amino acid is a common mutation observed in nature, it is generally thought to be disruptive to protein structure. Using a directed evolution approach, we find that the enzyme TEM-1 β-lactamase was broadly tolerant to the deletion mutations sampled. Circa 73% of the variants analysed retained activity towards ampicillin, with deletion mutations observed in helices and strands as well as regions important for structure and function. Several deletion variants had enhanced activity towards ceftazidime compared to the wild-type TEM-1 demonstrating that removal of an amino acid can have a beneficial outcome.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Publisher: Elsevier
ISSN: 0014-5793
Last Modified: 04 Jun 2017 06:45
URI: http://orca-mwe.cf.ac.uk/id/eprint/64411

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