1VYB

Endonuclease domain of human LINE1 ORF2p

Summary for 1VYB

• Entry DOI: 10.2210/pdb1vyb/pdb
• Descriptor: ORF2 CONTAINS A REVERSE TRANSCRIPTASE DOMAIN, SULFATE ION, SULFITE ION, ... (5 entities in total)
• Functional Keywords: endonuclease, ape-1 type, retrotransposition, retrotransposon, transferase, rna-directed dna polymerase
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 2
• Total formula weight: 55227.15

Authors

Weichenrieder, O.,Repanas, K.,Perrakis, A. (deposition date: 2004-04-25, release date: 2004-06-04, Last modification date: 2023-12-13)

Primary citation

Weichenrieder, O.,Repanas, K.,Perrakis, A.
Crystal structure of the targeting endonuclease of the human LINE-1 retrotransposon.
Structure, 12:975-986, 2004

PubMed Abstract: The human L1 endonuclease (L1-EN) is encoded by the non-LTR retrotransposon LINE-1 (L1). L1 is responsible for more than 1.5 million retrotransposition events in the history of the human genome, contributing more than a quarter to human genomic DNA (L1 and Alu elements). L1-EN is related to the well-understood human DNA repair endonuclease APE1, and its nicking specificity is a major determinant for retrotransposon integration site selection. The crystal structure of human L1 endonuclease is the first of a retrotransposon-encoded protein and a prototype for retrotransposon-encoded endonucleases involved in target-primed reverse transcription. Structure-based endonuclease alignments reveal a conserved threonine in addition to previously identified invariant residues and suggest that DNA recognition proceeds via the accommodation of an extrahelical nucleotide within a pocket of the enzyme. The present analysis will help to refine phylogenetic and functional relationships among metal-dependent phosphohydrolases and provides a basis for manipulating non-LTR retrotransposon integration site selection.

PubMed: 15274918
DOI: 10.1016/j.str.2004.04.011

Experimental method

X-RAY DIFFRACTION (1.8 Å)