1OTC

THE O. NOVA TELOMERE END BINDING PROTEIN COMPLEXED WITH SINGLE STRAND DNA

Summary for 1OTC

• Entry DOI: 10.2210/pdb1otc/pdb
• Descriptor: DNA (5'-D(*GP*GP*GP*GP*TP*TP*TP*TP*GP*GP*GP*G)-3'), PROTEIN (TELOMERE-BINDING PROTEIN ALPHA SUBUNIT), PROTEIN (TELOMERE-BINDING PROTEIN BETA SUBUNIT), ... (4 entities in total)
• Functional Keywords: single strand dna binding protein, protein dna interactions, protein protein interactions, oligonucleotide and oligosaccharide binding fold, ob fold, telomeres, protein-dna complex, protein/dna
• Biological source: Sterkiella nova; More
• Cellular location: Nucleus: P29549 P16458
• Total number of polymer chains: 3
• Total formula weight: 88690.43

Authors

Horvath, M.P.,Schweiker, V.L.,Bevilacqua, J.M.,Ruggles, J.A.,Schultz, S.C. (deposition date: 1998-11-25, release date: 1999-04-12, Last modification date: 2023-12-27)

Primary citation

Horvath, M.P.,Schweiker, V.L.,Bevilacqua, J.M.,Ruggles, J.A.,Schultz, S.C.
Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA.
Cell(Cambridge,Mass.), 95:963-974, 1998

PubMed Abstract: Telomeres are specialized protein-DNA complexes that compose the ends of eukaryotic chromosomes. Telomeres protect chromosome termini from degradation and recombination and act together with telomerase to ensure complete genome replication. We have determined the crystal structure of the two-subunit Oxytricha nova telomere end binding protein (OnTEBP) complexed with single strand telomeric DNA at 2.8 A resolution. The structure reveals four oligonucleotide/oligosaccharide-binding folds, three of which form a deep cleft that binds the ssDNA, and a fourth that forms an unusual protein-protein interaction between the alpha and beta subunits. This structure provides a molecular description of how the two subunits of OnTEBP recognize and bind ssDNA to form a sequence-specific, telomeric nucleoprotein complex that caps the very 3' ends of chromosomes.

PubMed: 9875850
DOI: 10.1016/S0092-8674(00)81720-1

Experimental method

X-RAY DIFFRACTION (2.8 Å)