Lambda repressor is shown in complex with its operator sequence of DNA. Each monomer of the dimer contains 2 alpha helices, nearly at right angles, that interact with the DNA. This motif is typical of prokaryotic DNA-binding proteins, and is often called the "helix-turn-helix" motif. In this view the DNA is colored cyan. The repressor is colored monochrome gray, except for the two pairs of alpha helices exhibiting the motif, colored yellow and green. Calmodulin: A Calcium-Binding Protein This is the structure of calmodulin as it was determined from crystallography, with a long extended central alpha-helix. Two helix-loop-helix, calcium binding sites are located at end. This is also called the E-F hand motif. The calcium ions are shown in red, and one helix-loop-helix motif is shown in yellow. This is the structure of calmodulin shown in yellow determined by NMR, in the presence of a peptide from myosin light chain kinase, shown in green. The long central helix of calmodulin is now wrapped around its substrate. The calcium ions are shown in red, and one helix-loop-helix motif is shown in yellow. Next: a beta hairpin
In this view the DNA is colored cyan. The repressor is colored monochrome gray, except for the two pairs of alpha helices exhibiting the motif, colored yellow and green. Calmodulin: A Calcium-Binding Protein This is the structure of calmodulin as it was determined from crystallography, with a long extended central alpha-helix. Two helix-loop-helix, calcium binding sites are located at end. This is also called the E-F hand motif. The calcium ions are shown in red, and one helix-loop-helix motif is shown in yellow. This is the structure of calmodulin shown in yellow determined by NMR, in the presence of a peptide from myosin light chain kinase, shown in green. The long central helix of calmodulin is now wrapped around its substrate. The calcium ions are shown in red, and one helix-loop-helix motif is shown in yellow. Next: a beta hairpin
This is the structure of calmodulin as it was determined from crystallography, with a long extended central alpha-helix. Two helix-loop-helix, calcium binding sites are located at end. This is also called the E-F hand motif. The calcium ions are shown in red, and one helix-loop-helix motif is shown in yellow. This is the structure of calmodulin shown in yellow determined by NMR, in the presence of a peptide from myosin light chain kinase, shown in green. The long central helix of calmodulin is now wrapped around its substrate. The calcium ions are shown in red, and one helix-loop-helix motif is shown in yellow. Next: a beta hairpin
The calcium ions are shown in red, and one helix-loop-helix motif is shown in yellow. This is the structure of calmodulin shown in yellow determined by NMR, in the presence of a peptide from myosin light chain kinase, shown in green. The long central helix of calmodulin is now wrapped around its substrate. The calcium ions are shown in red, and one helix-loop-helix motif is shown in yellow. Next: a beta hairpin
This is the structure of calmodulin shown in yellow determined by NMR, in the presence of a peptide from myosin light chain kinase, shown in green. The long central helix of calmodulin is now wrapped around its substrate. The calcium ions are shown in red, and one helix-loop-helix motif is shown in yellow. Next: a beta hairpin
The calcium ions are shown in red, and one helix-loop-helix motif is shown in yellow. Next: a beta hairpin
Next: a beta hairpin