1IGN

DNA-BINDING DOMAIN OF RAP1 IN COMPLEX WITH TELOMERIC DNA SITE

Summary for 1IGN

• Entry DOI: 10.2210/pdb1ign/pdb
• Descriptor: DNA (5'-D(*CP*CP*GP*CP*AP*CP*AP*CP*CP*CP*AP*CP*AP*CP*AP*CP*C P*AP*G)-3'), DNA (5'-D(*CP*CP*TP*GP*GP*TP*GP*TP*GP*TP*GP*GP*GP*TP*GP*TP*G P*CP*G)-3'), PROTEIN (RAP1), ... (4 entities in total)
• Functional Keywords: rap1, yeast, telomeres, homoeodomain, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus : P11938
• Total number of polymer chains: 6
• Total formula weight: 80635.28

Authors

Koenig, P.,Giraldo, R.,Chapman, L.,Rhodes, D. (deposition date: 1996-02-29, release date: 1997-01-27, Last modification date: 2024-02-07)

Primary citation

Konig, P.,Giraldo, R.,Chapman, L.,Rhodes, D.
The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA.
Cell(Cambridge,Mass.), 85:125-136, 1996

PubMed 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.

PubMed: 8620531
DOI: 10.1016/S0092-8674(00)81088-0

Experimental method

X-RAY DIFFRACTION (2.25 Å)