This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1wdu
From Proteopedia
| |||||||
| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 14:55:42 2008
