4c1a: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Coiled coil domain of the ZfL2-1 ORF1 protein from the zebrafish ZfL2- 1 retrotransposon== | ==Coiled coil domain of the ZfL2-1 ORF1 protein from the zebrafish ZfL2- 1 retrotransposon== | ||
<StructureSection load='4c1a' size='340' side='right' caption='[[4c1a]], [[Resolution|resolution]] 1.55Å' scene=''> | <StructureSection load='4c1a' size='340' side='right' caption='[[4c1a]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
| Line 5: | Line 6: | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c1b|4c1b]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c1b|4c1b]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c1a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c1a RCSB], [http://www.ebi.ac.uk/pdbsum/4c1a PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c1a OCA], [http://pdbe.org/4c1a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c1a RCSB], [http://www.ebi.ac.uk/pdbsum/4c1a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c1a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 15: | Line 16: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4c1a" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 22:46, 11 August 2016
Coiled coil domain of the ZfL2-1 ORF1 protein from the zebrafish ZfL2- 1 retrotransposonCoiled coil domain of the ZfL2-1 ORF1 protein from the zebrafish ZfL2- 1 retrotransposon
Structural highlights
Publication Abstract from PubMedNon-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. Structure and properties of the esterase from non-LTR retrotransposons suggest a role for lipids in retrotransposition.,Schneider AM, Schmidt S, Jonas S, Vollmer B, Khazina E, Weichenrieder O Nucleic Acids Res. 2013 Sep 3. PMID:24003030[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||