1XJV

Crystal structure of human POT1 bound to telomeric single-stranded DNA (TTAGGGTTAG)

Summary for 1XJV

• Entry DOI: 10.2210/pdb1xjv/pdb
• Descriptor: hT10 d(TTAGGGTTAG), Protection of telomeres 1 (3 entities in total)
• Functional Keywords: telomere; protein-dna complex; single-stranded dna, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q9NUX5
• Total number of polymer chains: 2
• Total formula weight: 36312.12

Authors

Lei, M.,Podell, E.R.,Cech, T.R. (deposition date: 2004-09-25, release date: 2004-12-14, Last modification date: 2024-02-14)

Primary citation

Lei, M.,Podell, E.R.,Cech, T.R.
Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection
Nat.Struct.Mol.Biol., 11:1223-1229, 2004

PubMed Abstract: The POT1 (protection of telomeres 1) protein binds the single-stranded overhang at the ends of chromosomes in diverse eukaryotes. It is essential for chromosome end-protection in the fission yeast Schizosaccharomyces pombe, and it is involved in regulation of telomere length in human cells. Here, we report the crystal structure at a resolution of 1.73 A of the N-terminal half of human POT1 (hPOT1) protein bound to a telomeric single-stranded DNA (ssDNA) decamer, TTAGGGTTAG, the minimum tight-binding sequence indicated by in vitro binding assays. The structure reveals that hPOT1 contains two oligonucleotide/ oligosaccharide-binding (OB) folds; the N-terminal OB fold binds the first six nucleotides, resembling the structure of the S. pombe Pot1pN-ssDNA complex, whereas the second OB fold binds and protects the 3' end of the ssDNA. These results provide an atomic-resolution model for chromosome end-capping.

PubMed: 15558049
DOI: 10.1038/nsmb867

Experimental method

X-RAY DIFFRACTION (1.73 Å)