3K6G

Crystal structure of Rap1 and TRF2 complex

Summary for 3K6G

• Entry DOI: 10.2210/pdb3k6g/pdb
• Descriptor: Telomeric repeat-binding factor 2-interacting protein 1, Telomeric repeat-binding factor 2 (3 entities in total)
• Functional Keywords: helix, chromosomal protein, nucleus, phosphoprotein, telomere, cell cycle, dna-binding, protein binding
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q9NYB0 Q15554
• Total number of polymer chains: 6
• Total formula weight: 50182.16

Authors

Chen, Y.,Rai, R.,Yang, Y.T.,Zheng, H.,Chang, S.,Lei, M. (deposition date: 2009-10-08, release date: 2010-10-13, Last modification date: 2011-07-13)

Primary citation

Chen, Y.,Rai, R.,Zhou, Z.R.,Kanoh, J.,Ribeyre, C.,Yang, Y.,Zheng, H.,Damay, P.,Wang, F.,Tsujii, H.,Hiraoka, Y.,Shore, D.,Hu, H.Y.,Chang, S.,Lei, M.
A conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organisms.
Nat.Struct.Mol.Biol., 18:213-221, 2011

PubMed Abstract: Repressor activator protein 1 (RAP1) is the most highly conserved telomere protein. It is involved in protecting chromosome ends in fission yeast and promoting gene silencing in Saccharomyces cerevisiae, whereas it represses homology-directed recombination at telomeres in mammals. To understand how RAP1 has such diverse functions at telomeres, we solved the crystal or solution structures of the RAP1 C-terminal (RCT) domains of RAP1 from multiple organisms in complex with their respective protein-binding partners. Our analysis establishes RAP1(RCT) as an evolutionarily conserved protein-protein interaction module. In mammalian and fission yeast cells, this module interacts with TRF2 and Taz1, respectively, targeting RAP1 to chromosome ends for telomere protection. In contrast, S. cerevisiae RAP1 uses its RCT domain to recruit Sir3 to telomeres to mediate gene silencing. Together, our results show that, depending on the organism, the evolutionarily conserved RAP1 RCT motif has diverse functional roles at telomeres.

PubMed: 21217703
DOI: 10.1038/nsmb.1974

Experimental method

X-RAY DIFFRACTION (1.95 Å)