Structure of the amino-terminal domain of phage 434 repressor at 2.0 A resolution

J Mol Biol. 1989 Jan 5;205(1):189-200. doi: 10.1016/0022-2836(89)90375-6.

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

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacteriophages / genetics*
  • DNA-Binding Proteins / genetics
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Repressor Proteins / genetics*
  • Transcription Factors / genetics*
  • Viral Proteins / genetics*
  • Viral Regulatory and Accessory Proteins
  • X-Ray Diffraction

Substances

  • DNA-Binding Proteins
  • Repressor Proteins
  • Transcription Factors
  • Viral Proteins
  • Viral Regulatory and Accessory Proteins
  • phage repressor proteins