3UKG

Crystal structure of Rap1/DNA complex

Summary for 3UKG

• Entry DOI: 10.2210/pdb3ukg/pdb
• Descriptor: DNA-binding protein RAP1, telomeric DNA, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: double myb, transcription regulation, telomeres length regulation, telomeres protection, nucleus, 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: 3
• Total formula weight: 47475.13

Authors

Matot, B.,Le Bihan, Y.-V.,Gasparini, S.,LeDu, M.H. (deposition date: 2011-11-09, release date: 2011-12-07, Last modification date: 2023-09-13)

Primary citation

Matot, B.,Le Bihan, Y.V.,Lescasse, R.,Perez, J.,Miron, S.,David, G.,Castaing, B.,Weber, P.,Raynal, B.,Zinn-Justin, S.,Gasparini, S.,Le Du, M.H.
The orientation of the C-terminal domain of the Saccharomyces cerevisiae Rap1 protein is determined by its binding to DNA.
Nucleic Acids Res., 40:3197-3207, 2012

PubMed Abstract: Rap1 is an essential DNA-binding factor from the yeast Saccharomyces cerevisiae involved in transcription and telomere maintenance. Its binding to DNA targets Rap1 at particular loci, and may optimize its ability to form functional macromolecular assemblies. It is a modular protein, rich in large potentially unfolded regions, and comprising BRCT, Myb and RCT well-structured domains. Here, we present the architectures of Rap1 and a Rap1/DNA complex, built through a step-by-step integration of small angle X-ray scattering, X-ray crystallography and nuclear magnetic resonance data. Our results reveal Rap1 structural adjustment upon DNA binding that involves a specific orientation of the C-terminal (RCT) domain with regard to the DNA binding domain (DBD). Crystal structure of DBD in complex with a long DNA identifies an essential wrapping loop, which constrains the orientation of the RCT and affects Rap1 affinity to DNA. Based on our structural information, we propose a model for Rap1 assembly at telomere.

PubMed: 22139930
DOI: 10.1093/nar/gkr1166

Experimental method

X-RAY DIFFRACTION (2.95 Å)