Two structures of a lambda Cro variant highlight dimer flexibility but disfavor major dimer distortions upon specific binding of cognate DNA.

Abstract excerpt

Previously reported crystal structures of free and DNA-bound dimers of lambda Cro differ strongly (about 4 A backbone rmsd), suggesting both flexibility of the dimer interface and induced-fit protein structure changes caused by sequence-specific DNA binding. Here, we present two crystal structures, in space groups P3(2)21 and C2 at 1.35 and 1.40 A resolution, respectively, of a variant of lambda Cro with three...

Topics

• Bacteriophage lambda
• Crystallography, X-Ray
• DNA, Viral
• DNA-Binding Proteins
• Dimerization
• Escherichia coli
• Genetic Variation
• Helix-Turn-Helix Motifs
• Hydrogen Bonding
• Hydrogen-Ion Concentration
• Hydrophobic and Hydrophilic Interactions
• Models, Chemical