4C1B
Esterase domain of the ZfL2-1 ORF1 protein from the zebrafish ZfL2-1 retrotransposon
Summary for 4C1B
| Entry DOI | 10.2210/pdb4c1b/pdb |
| Related | 4C1A |
| Descriptor | ORF1-ENCODED PROTEIN (2 entities in total) |
| Functional Keywords | hydrolase, retrotransposition, rna-binding, membrane-binding, lipid-binding, self-association |
| Biological source | DANIO RERIO (ZEBRAFISH) |
| Total number of polymer chains | 3 |
| Total formula weight | 57423.28 |
| Authors | Schneider, A.M.,Weichenrieder, O. (deposition date: 2013-08-11, release date: 2013-09-11, Last modification date: 2024-05-08) |
| Primary citation | 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 Cited by 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: 24003030DOI: 10.1093/NAR/GKT786 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.501 Å) |
Structure validation
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