Abstract
The crystal structure of the amino-terminal domain of phage 434 repressor has been solved using molecular replacement methods and refined to an R-factor of 19.3% against data to 2.0 A resolution. The protein comprises five short alpha-helices. Two of these form a helix-turn-helix motif, very similar to those found in related proteins. The protein is remarkably similar to the Cro protein from the same phage.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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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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Bacteriophages / genetics*
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DNA-Binding Proteins / genetics
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Models, Molecular
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Molecular Sequence Data
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Protein Conformation
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Repressor Proteins / genetics*
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Transcription Factors / genetics*
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Viral Proteins / genetics*
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Viral Regulatory and Accessory Proteins
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X-Ray Diffraction
Substances
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DNA-Binding Proteins
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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