1wdu

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(New page: 200px<br /><applet load="1wdu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wdu, resolution 2.4&Aring;" /> '''Endonuclease domain o...)
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[[Image:1wdu.gif|left|200px]]<br /><applet load="1wdu" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1wdu, resolution 2.4&Aring;" />
caption="1wdu, resolution 2.4&Aring;" />
'''Endonuclease domain of TRAS1, a telomere-specific non-LTR retrotransposon'''<br />
'''Endonuclease domain of TRAS1, a telomere-specific non-LTR retrotransposon'''<br />
==Overview==
==Overview==
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The telomere-specific long interspersed nuclear element, TRAS1, encodes an, endonuclease domain, TRAS1-EN, which specifically cleaves the telomeric, repeat targets (TTAGG)n of insects and (TTAGGG)n of vertebrates. To, elucidate the sequence-specific recognition properties of TRAS1-EN, we, determined the crystal structure at 2.4-A resolution. TRAS1-EN has a, four-layered alpha/beta sandwich structure; its topology is similar to, apurinic/apyrimidinic endonucleases, but the beta-hairpin (beta10-beta11), at the edge of the DNA-binding surface makes an extra loop that, distinguishes TRAS1-EN from cellular apurinic/apyrimidinic endonucleases., A protein-DNA complex model suggests that the beta10-beta11 hairpin fits, into the minor groove, enabling interaction with the telomeric repeats., Mutational studies of TRAS1-EN also indicated that the Asp-130 and, beta10-beta11 hairpin structure are involved in specific recognition of, telomeric repeats.
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The telomere-specific long interspersed nuclear element, TRAS1, encodes an endonuclease domain, TRAS1-EN, which specifically cleaves the telomeric repeat targets (TTAGG)n of insects and (TTAGGG)n of vertebrates. To elucidate the sequence-specific recognition properties of TRAS1-EN, we determined the crystal structure at 2.4-A resolution. TRAS1-EN has a four-layered alpha/beta sandwich structure; its topology is similar to apurinic/apyrimidinic endonucleases, but the beta-hairpin (beta10-beta11) at the edge of the DNA-binding surface makes an extra loop that distinguishes TRAS1-EN from cellular apurinic/apyrimidinic endonucleases. A protein-DNA complex model suggests that the beta10-beta11 hairpin fits into the minor groove, enabling interaction with the telomeric repeats. Mutational studies of TRAS1-EN also indicated that the Asp-130 and beta10-beta11 hairpin structure are involved in specific recognition of telomeric repeats.
==About this Structure==
==About this Structure==
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1WDU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori] with PO4 and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WDU OCA].
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1WDU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WDU OCA].
==Reference==
==Reference==
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[[Category: four-layered alpha/beta sandwich]]
[[Category: four-layered alpha/beta sandwich]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:48:17 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:43:17 2008''

Revision as of 13:43, 21 February 2008


1wdu, resolution 2.4Å

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Endonuclease domain of TRAS1, a telomere-specific non-LTR retrotransposon

Overview

The telomere-specific long interspersed nuclear element, TRAS1, encodes an endonuclease domain, TRAS1-EN, which specifically cleaves the telomeric repeat targets (TTAGG)n of insects and (TTAGGG)n of vertebrates. To elucidate the sequence-specific recognition properties of TRAS1-EN, we determined the crystal structure at 2.4-A resolution. TRAS1-EN has a four-layered alpha/beta sandwich structure; its topology is similar to apurinic/apyrimidinic endonucleases, but the beta-hairpin (beta10-beta11) at the edge of the DNA-binding surface makes an extra loop that distinguishes TRAS1-EN from cellular apurinic/apyrimidinic endonucleases. A protein-DNA complex model suggests that the beta10-beta11 hairpin fits into the minor groove, enabling interaction with the telomeric repeats. Mutational studies of TRAS1-EN also indicated that the Asp-130 and beta10-beta11 hairpin structure are involved in specific recognition of telomeric repeats.

About this Structure

1WDU is a Single protein structure of sequence from Bombyx mori with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the endonuclease domain encoded by the telomere-specific long interspersed nuclear element, TRAS1., Maita N, Anzai T, Aoyagi H, Mizuno H, Fujiwara H, J Biol Chem. 2004 Sep 24;279(39):41067-76. Epub 2004 Jul 9. PMID:15247245

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