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| | <StructureSection load='2w7a' size='340' side='right'caption='[[2w7a]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='2w7a' size='340' side='right'caption='[[2w7a]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2w7a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W7A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2W7A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2w7a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W7A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W7A FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2w7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w7a OCA], [http://pdbe.org/2w7a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2w7a RCSB], [http://www.ebi.ac.uk/pdbsum/2w7a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2w7a ProSAT]</span></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=2w7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w7a OCA], [https://pdbe.org/2w7a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w7a RCSB], [https://www.ebi.ac.uk/pdbsum/2w7a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w7a ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/LORF1_HUMAN LORF1_HUMAN] Nucleic acid-binding protein which is essential for retrotransposition of LINE-1 elements in the genome. May function as a nucleic acid chaperone binding its own transcript and therefore preferentially mobilizing the transcript from which they are encoded.<ref>PMID:11158327</ref> <ref>PMID:21937507</ref> <ref>PMID:8945518</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w7/2w7a_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w7/2w7a_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Khazina, E]] | + | [[Category: Khazina E]] |
| - | [[Category: Weichenrieder, O]] | + | [[Category: Weichenrieder O]] |
| - | [[Category: Rna binding protein]]
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| - | [[Category: Rna-binding protein]]
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| Structural highlights
Function
LORF1_HUMAN Nucleic acid-binding protein which is essential for retrotransposition of LINE-1 elements in the genome. May function as a nucleic acid chaperone binding its own transcript and therefore preferentially mobilizing the transcript from which they are encoded.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Non-LTR retrotransposons (NLRs) are a unique class of mobile genetic elements that have significant impact on the evolution of eukaryotic genomes. However, the molecular details and functions of their encoded proteins, in particular of the accessory ORF1p proteins, are poorly understood. Here, we identify noncanonical RNA-recognition-motifs (RRMs) in several phylogenetically unrelated NLR ORF1p proteins. This provides an explanation for their RNA-binding properties and clearly shows that they are not related to the retroviral nucleocapsid protein Gag, despite the frequent presence of CCHC zinc knuckles. In particular, we characterize the ORF1p protein of the human long interspersed nuclear element 1 (LINE-1 or L1). We show that L1ORF1p is a multidomain protein, consisting of a coiled coil (cc), RRM, and C-terminal domain (CTD). Most importantly, we solved the crystal structure of the RRM domain, which is characterized by extended loops stabilized by unique salt bridges. Furthermore, we demonstrate that L1ORF1p trimerizes via its N-terminal cc domain, and we suggest that this property is functionally important for all homologues. The formation of distinct complexes with single-stranded nucleic acids requires the presence of the RRM and CTD domains on the same polypeptide chain as well as their close cooperation. Finally, the phylogenetic analysis of mammalian L1ORF1p shows an ancient origin of the RRM domain and supports a modular evolution of NLRs.
Non-LTR retrotransposons encode noncanonical RRM domains in their first open reading frame.,Khazina E, Weichenrieder O Proc Natl Acad Sci U S A. 2009 Jan 20;106(3):731-6. Epub 2009 Jan 12. PMID:19139409[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wei W, Gilbert N, Ooi SL, Lawler JF, Ostertag EM, Kazazian HH, Boeke JD, Moran JV. Human L1 retrotransposition: cis preference versus trans complementation. Mol Cell Biol. 2001 Feb;21(4):1429-39. PMID:11158327 doi:http://dx.doi.org/10.1128/MCB.21.4.1429-1439.2001
- ↑ Callahan KE, Hickman AB, Jones CE, Ghirlando R, Furano AV. Polymerization and nucleic acid-binding properties of human L1 ORF1 protein. Nucleic Acids Res. 2012 Jan;40(2):813-27. doi: 10.1093/nar/gkr728. Epub 2011 Sep , 21. PMID:21937507 doi:http://dx.doi.org/10.1093/nar/gkr728
- ↑ Moran JV, Holmes SE, Naas TP, DeBerardinis RJ, Boeke JD, Kazazian HH Jr. High frequency retrotransposition in cultured mammalian cells. Cell. 1996 Nov 29;87(5):917-27. PMID:8945518
- ↑ Khazina E, Weichenrieder O. Non-LTR retrotransposons encode noncanonical RRM domains in their first open reading frame. Proc Natl Acad Sci U S A. 2009 Jan 20;106(3):731-6. Epub 2009 Jan 12. PMID:19139409
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