ArticleProtein science : a publication of the Protein Society2009
Re-engineering a beta-lactamase using prototype peptides from a library of local structural motifs.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Fifty years of biophysics in Argentina.Biophysical reviews · 2023Article
- Equilibrium partially folded states of B. licheniformisEuropean biophysics journal : EBJ · 2019Article
- X-ray evidence of a native state with increased compactness populated by tryptophan-less B. licheniformis β-lactamase.Protein science : a publication of the Protein Society · 2012Article
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Authors and funding
3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
B. licheniformis exo-small beta-lactamase (ESBL) has a complex architecture with twelve alpha helices and a five-stranded beta sheet. We replaced, separately or simultaneously, three of the ESBL alpha helices with prototype amphiphatic helices from a catalog of secondary structure elements. Although the substitutes bear no sequence similarity to the originals and pertain to unrelated protein families, all the engineered ESBL variants were found able to fold in native like structures with in vitro and in vivo enzymic activity. The triple substituted variant resembles a primitive protein, with folding defects such as a strong tendency to oligomerization and very low stability; however it mimics a non homologous recombinant abandoning the family sequence space while preserving fold. The results test protein folding and evolution theories.
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