1wdu | pdb_00001wdu

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

spinqualitylabelsall models 1wdu, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1wdu is a 2 chain structure with sequence from Bommo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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