2CKX

Crystal structure of NgTRF1, double-stranded telomeric repeat binding factor from Nicotiana tabacum.

Summary for 2CKX

• Entry DOI: 10.2210/pdb2ckx/pdb
• Descriptor: TELOMERE BINDING PROTEIN TBP1 (2 entities in total)
• Functional Keywords: nuclear protein
• Biological source: NICOTIANA TABACUM (TOBACCO)
• Total number of polymer chains: 1
• Total formula weight: 9594.80

Authors

Byun, J.-S.,Cho, H.-S. (deposition date: 2006-04-24, release date: 2007-05-29, Last modification date: 2024-05-08)

Primary citation

Ko, S.,Jun, S.,Bae, H.,Byun, J.-S.,Han, W.,Park, H.,Yang, S.W.,Park, S.,Jeon, Y.H.,Cheong, C.,Kim, W.T.,Lee, W.,Cho, H.-S.
Structure of the DNA-Binding Domain of Ngtrf1 Reveals Unique Features of Plant Telomere-Binding Proteins.
Nucleic Acids Res., 36:2739-, 2008

PubMed Abstract: Telomeres are protein-DNA elements that are located at the ends of linear eukaryotic chromosomes. In concert with various telomere-binding proteins, they play an essential role in genome stability. We determined the structure of the DNA-binding domain of NgTRF1, a double-stranded telomere-binding protein of tobacco, using multidimensional NMR spectroscopy and X-ray crystallography. The DNA-binding domain of NgTRF1 contained the Myb-like domain and C-terminal Myb-extension that is characteristic of plant double-stranded telomere-binding proteins. It encompassed amino acids 561-681 (NgTRF1(561-681)), and was composed of 4 alpha-helices. We also determined the structure of NgTRF1(561-681) bound to plant telomeric DNA. We identified several amino acid residues that interacted directly with DNA, and confirmed their role in the binding of NgTRF1 to telomere using site-directed mutagenesis. Based on a structural comparison of the DNA-binding domains of NgTRF1 and human TRF1 (hTRF1), NgTRF1 has both common and unique DNA-binding properties. Interaction of Myb-like domain with telomeric sequences is almost identical in NgTRF1(561-681) with the DNA-binding domain of hTRF1. The interaction of Arg-638 with the telomeric DNA, which is unique in NgTRF1(561-681), may provide the structural explanation for the specificity of NgTRF1 to the plant telomere sequences, (TTTAGGG)(n).

PubMed: 18367475
DOI: 10.1093/NAR/GKN030

Experimental method

X-RAY DIFFRACTION (1.9 Å)