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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[[Image:1kix.gif|left|200px]]<br /><applet load="1kix" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1kix, resolution 2.70&Aring;" />
caption="1kix, resolution 2.70&Aring;" />
'''Dimeric Structure of the O. nova Telomere End Binding Protein Alpha Subunit with Bound ssDNA'''<br />
'''Dimeric Structure of the O. nova Telomere End Binding Protein Alpha Subunit with Bound ssDNA'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1KIX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sterkiella_nova Sterkiella nova] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KIX OCA].
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1KIX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sterkiella_nova Sterkiella nova] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KIX OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sterkiella nova]]
[[Category: Sterkiella nova]]
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[[Category: Peersen, O.B.]]
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[[Category: Peersen, O B.]]
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[[Category: Ruggles, J.A.]]
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[[Category: Ruggles, J A.]]
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[[Category: Schultz, S.C.]]
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[[Category: Schultz, S C.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: dna-protein interactions]]
[[Category: dna-protein interactions]]
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[[Category: telomere binding protein]]
[[Category: telomere binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:16:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:34:38 2008''

Revision as of 11:34, 21 February 2008


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 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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