4C1A

Coiled coil domain of the ZfL2-1 ORF1 protein from the zebrafish ZfL2- 1 retrotransposon

4C1A の概要

• エントリーDOI: 10.2210/pdb4c1a/pdb
• 関連するPDBエントリー: 4C1B
• 分子名称: ORF1-ENCODED PROTEIN, GLYCEROL (3 entities in total)
• 機能のキーワード: hydrolase, retrotransposition, rna-binding, membrane-binding, lipid-binding, self-association
• 由来する生物種: DANIO RERIO (ZEBRAFISH)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 17003.80

構造登録者

Schneider, A.M.,Weichenrieder, O. (登録日: 2013-08-11, 公開日: 2013-09-11, 最終更新日: 2023-12-20)

主引用文献

Schneider, A.M.,Schmidt, S.,Jonas, S.,Vollmer, B.,Khazina, E.,Weichenrieder, O.
Structure and Properties of the Esterase from Non-Ltr Retrotransposons Suggest a Role for Lipids in Retrotransposition.
Nucleic Acids Res., 41:10563-, 2013

PubMed Abstract: Non-LTR retrotransposons are mobile genetic elements and play a major role in eukaryotic genome evolution and disease. Similar to retroviruses they encode a reverse transcriptase, but their genomic integration mechanism is fundamentally different, and they lack homologs of the retroviral nucleocapsid-forming protein Gag. Instead, their first open reading frames encode distinct multi-domain proteins (ORF1ps) presumed to package the retrotransposon-encoded RNA into ribonucleoprotein particles (RNPs). The mechanistic roles of ORF1ps are poorly understood, particularly of ORF1ps that appear to harbor an enzymatic function in the form of an SGNH-type lipolytic acetylesterase. We determined the crystal structures of the coiled coil and esterase domains of the ORF1p from the Danio rerio ZfL2-1 element. We demonstrate a dimerization of the coiled coil and a hydrolytic activity of the esterase. Furthermore, the esterase binds negatively charged phospholipids and liposomes, but not oligo-(A) RNA. Unexpectedly, the esterase can split into two dynamic half-domains, suited to engulf long fatty acid substrates extending from the active site. These properties indicate a role for lipids and membranes in non-LTR retrotransposition. We speculate that Gag-like membrane targeting properties of ORF1ps could play a role in RNP assembly and in membrane-dependent transport or localization processes.

PubMed: 24003030
DOI: 10.1093/NAR/GKT786

実験手法

X-RAY DIFFRACTION (1.55 Å)