SNAP annotations: PDB entry 1ign

PDB-id

1ign; DSSR-derived features in text and JSON formats; DNAproDB

Class

DNA binding protein-DNA

Method

X-ray (2.25 Å)

Summary

DNA-binding domain of rap1 in complex with telomeric DNA site

Reference

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.

Abstract

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.