1WDU

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

Summary for 1WDU

• Entry DOI: 10.2210/pdb1wdu/pdb
• Descriptor: TRAS1 ORF2p, PHOSPHATE ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: four-layered alpha/beta sandwich, rna binding protein
• Biological source: Bombyx mori (domestic silkworm)
• Total number of polymer chains: 2
• Total formula weight: 55178.44

Authors

Maita, N.,Anzai, T.,Aoyagi, H.,Mizuno, H.,Fujiwara, H. (deposition date: 2004-05-17, release date: 2004-08-10, Last modification date: 2024-05-29)

Primary citation

Maita, N.,Anzai, T.,Aoyagi, H.,Mizuno, H.,Fujiwara, H.
Crystal structure of the endonuclease domain encoded by the telomere-specific long interspersed nuclear element, TRAS1
J.Biol.Chem., 279:41067-41076, 2004

PubMed Abstract: 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.

PubMed: 15247245
DOI: 10.1074/jbc.M406556200

Experimental method

X-RAY DIFFRACTION (2.4 Å)