1otc: Difference between revisions

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[[Image:1otc.gif|left|200px]]
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{{STRUCTURE_1otc|  PDB=1otc  |  SCENE=  }}  
{{STRUCTURE_1otc|  PDB=1otc  |  SCENE=  }}  


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




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Single strand dna binding protein]]
[[Category: Single strand dna binding protein]]
[[Category: Telomere]]
[[Category: Telomere]]
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Revision as of 00:29, 29 July 2008

File:1otc.png

Template:STRUCTURE 1otc

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

Template:ABSTRACT PUBMED 9875850

About this StructureAbout this Structure

1OTC is a Protein complex structure of sequences from Sterkiella nova. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA., Horvath MP, Schweiker VL, Bevilacqua JM, Ruggles JA, Schultz SC, Cell. 1998 Dec 23;95(7):963-74. PMID:9875850

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