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| | <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=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4c1a]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Brachidanio_rerio Brachidanio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C1A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C1A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4c1a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C1A FirstGlance]. <br> |
| - | </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" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4c1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c1a OCA], [https://pdbe.org/4c1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c1a RCSB], [https://www.ebi.ac.uk/pdbsum/4c1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c1a ProSAT]</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;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [[https://www.uniprot.org/uniprot/Q3LG57_DANRE Q3LG57_DANRE]] |
| - | 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.
| + | |
| - | | + | |
| - | 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<ref>PMID:24003030</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 4c1a" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Brachidanio rerio]] | + | [[Category: Danio rerio]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Schneider, A M]] | + | [[Category: Schneider AM]] |
| - | [[Category: Weichenrieder, O]] | + | [[Category: Weichenrieder O]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Lipid-binding]]
| + | |
| - | [[Category: Membrane-binding]]
| + | |
| - | [[Category: Retrotransposition]]
| + | |
| - | [[Category: Rna-binding]]
| + | |
| - | [[Category: Self-association]]
| + | |
