Abstract
lambda Cro is a dimeric DNA binding protein. Random mutagenesis and a selection for Cro activity have been used to identify the contacts between Cro subunits that are crucial for maintenance of a stably folded structure. To obtain equivalent contacts in a monomeric system, a Cro variant was designed and constructed in which the antiparallel beta-ribbon that forms the dimer interface was replaced by a beta-hairpin. The engineered monomer has a folded structure similar to wild type, is significantly more stable than wild type, and exhibits novel half-operator binding activity.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Bacteriophage lambda / genetics*
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Circular Dichroism
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DNA-Binding Proteins*
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Escherichia coli / genetics
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Genetic Variation*
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Macromolecular Substances
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Models, Molecular
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Molecular Sequence Data
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Mutagenesis
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Protein Conformation
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Repressor Proteins / genetics*
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Repressor Proteins / metabolism
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Thermodynamics
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Transcription Factors / genetics*
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Viral Proteins
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Viral Regulatory and Accessory Proteins
Substances
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DNA-Binding Proteins
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Macromolecular Substances
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Repressor Proteins
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Transcription Factors
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Viral Proteins
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Viral Regulatory and Accessory Proteins
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phage repressor proteins