Summary information and primary citation

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DNA binding protein-DNA
X-ray (2.25 Å)
DNA-binding domain of rap1 in complex with telomeric DNA site
Konig P, Giraldo R, Chapman L, Rhodes D (1996): "The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA." Cell(Cambridge,Mass.), 85, 125-136. doi: 10.1016/S0092-8674(00)81088-0.
Telomeres, the nucleoprotein complexes at the ends of eukaryotic chromosomes, are essential for chromosome stability. In the yeast S. cerevisiae, telomeric DNA is bound in a sequence-specific manner by RAP1, a multifunctional protein also involved in transcriptional regulation. Here we report the crystal structure of the DNA-binding domain of RAP1 in complex with telomeric DNA site at 2.25 A resolution. The protein contains two similar domains that bind DNA in a tandem orientation, recognizing a tandemly repeated DNA sequence. The domains are structurally related to the homeodomain and the proto-oncogene Myb, but show novel features in their DNA-binding mode. A structured linker between the domains and a long C-terminal tail contribute to the binding specificity. This structure provides insight into the recognition of the conserved telomeric DNA sequences by a protein.

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