Re-engineering a beta-lactamase using prototype peptides from a library of local structural motifs.
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ABSTRACT:
SUBMITTER: Risso VA
PROVIDER: S-EPMC2708064 | biostudies-literature | 2009 Feb
REPOSITORIES: biostudies-literature
Publications
Re-engineering a beta-lactamase using prototype peptides from a library of local structural motifs.
Risso Valeria A VA Primo María E ME Ermácora Mario R MR
Protein science : a publication of the Protein Society 20090201 2
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 vitr ...[more]
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