2YKO

Structure of the human LINE-1 ORF1p trimer

2YKO の概要

• エントリーDOI: 10.2210/pdb2yko/pdb
• 関連するPDBエントリー: 2JRB 2LDY 2W7A 2YKP 2YKQ
• 分子名称: LINE-1 ORF1P, CHLORIDE ION (3 entities in total)
• 機能のキーワード: rna-binding protein, genome evolution, nucleic acid chaperone, rnp, coiled-coil, rna binding protein
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 84141.12

構造登録者

Khazina, E.,Weichenrieder, O. (登録日: 2011-05-28, 公開日: 2011-08-10, 最終更新日: 2024-11-20)

主引用文献

Khazina, E.,Truffault, V.,Buettner, R.,Schmidt, S.,Coles, M.,Weichenrieder, O.
Trimeric Structure and Flexibility of the L1Orf1P Protein in Human L1 Retrotransposition
Nat.Struct.Mol.Biol., 18:1006-, 2011

PubMed Abstract: The LINE-1 (L1) retrotransposon emerges as a major source of human interindividual genetic variation, with important implications for evolution and disease. L1 retrotransposition is poorly understood at the molecular level, and the mechanistic details and evolutionary origin of the L1-encoded L1ORF1 protein (L1ORF1p) are particularly obscure. Here three crystal structures of trimeric L1ORF1p and NMR solution structures of individual domains reveal a sophisticated and highly structured, yet remarkably flexible, RNA-packaging protein. It trimerizes via an N-terminal, ion-containing coiled coil that serves as scaffold for the flexible attachment of the central RRM and the C-terminal CTD domains. The structures explain the specificity for single-stranded RNA substrates, and a mutational analysis indicates that the precise control of domain flexibility is critical for retrotransposition. Although the evolutionary origin of L1ORF1p remains unclear, our data reveal previously undetected structural and functional parallels to viral proteins.

PubMed: 21822284
DOI: 10.1038/NSMB.2097

実験手法

X-RAY DIFFRACTION (2.1 Å)