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Investigating protein structural plasticity by surveying the consequence of an amino acid deletion from TEM‐1 β‐lactamase
Author(s) -
Simm Alan M.,
Baldwin Amy J.,
Busse Kathy,
Jones D. Dafydd
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.07.018
Subject(s) - mutation , amino acid , enzyme , peptide sequence , protein structure , biology , structural plasticity , biochemistry , genetics , directed evolution , chemistry , function (biology) , ceftazidime , bacteria , gene , mutant , pseudomonas aeruginosa , neuroscience
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.