1kix

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(New page: 200px<br /><applet load="1kix" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kix, resolution 2.70&Aring;" /> '''Dimeric Structure of...)
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Revision as of 17:09, 20 November 2007


1kix, resolution 2.70Å

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Dimeric Structure of the O. nova Telomere End Binding Protein Alpha Subunit with Bound ssDNA

Overview

Telomeres are the specialized protein--DNA complexes that cap and protect, the ends of linear eukaryotic chromosomes. The extreme 3' end of the, telomeric DNA in Oxytricha nova is bound by a two-subunit, sequence-specific and 3' end-specific protein called the telomere, end-binding protein (OnTEBP). Here we describe the crystal structure of, the alpha-subunit of OnTEBP in complex with T4G4 single-stranded telomeric, DNA. This structure shows an (alpha--ssDNA)2 homodimer with a large, approximately 7,000 A2 protein--protein interface in which the domains of, alpha are rearranged extensively from their positions in the structure of, an alpha--beta--ssDNA ternary complex. The (alpha--ssDNA)2 complex can, bind two telomeres on opposite sides of the dimer and, thus, acts as a, protein mediator of telomere--telomere associations. The structures of the, (alpha--ssDNA)2 dimer presented here and the previously described, alpha--beta--ssDNA complex demonstrate that OnTEBP forms multiple, telomeric complexes that potentially mediate the assembly and disassembly, of higher order telomeric structures.

About this Structure

1KIX is a Single protein structure of sequence from Sterkiella nova with SO4 as ligand. Full crystallographic information is available from OCA.

Reference

Dimeric structure of the Oxytricha nova telomere end-binding protein alpha-subunit bound to ssDNA., Peersen OB, Ruggles JA, Schultz SC, Nat Struct Biol. 2002 Mar;9(3):182-7. PMID:11836536

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