6fia: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 6fia is ~~ON HOLD~~

==Structure of the human LINE-1 ORF1p coiled coil domain==

== Structural highlights ==

<table><tr><td colspan='2'>[[6fia]] is a 6 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=6FIA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FIA FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">L1RE1, LRE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6fia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fia OCA], [http://pdbe.org/6fia PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fia RCSB], [http://www.ebi.ac.uk/pdbsum/6fia PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fia ProSAT]</span></td></tr>

</table>

== Function ==

[[http://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>

== Publication Abstract from PubMed ==

LINE-1 (L1) is an autonomous retrotransposon, which acted throughout mammalian evolution and keeps contributing to human genotypic diversity, genetic disease and cancer. L1 encodes two essential proteins: L1ORF1p, a unique RNA-binding protein, and L1ORF2p, an endonuclease and reverse transcriptase. L1ORF1p contains an essential, but rapidly evolving N-terminal portion, homo-trimerizes via a coiled coil and packages L1RNA into large assemblies. Here, we determined crystal structures of the entire coiled coil domain of human L1ORF1p. We show that retrotransposition requires a non-ideal and metastable coiled coil structure, and a strongly basic L1ORF1p amino terminus. Human L1ORF1p therefore emerges as a highly calibrated molecular machine, sensitive to mutation but functional in different hosts. Our analysis rationalizes the locally rapid L1ORF1p sequence evolution and reveals striking mechanistic parallels to coiled coil-containing membrane fusion proteins. It also suggests how trimeric L1ORF1p could form larger meshworks and indicates critical novel steps in L1 retrotransposition.

~~Authors~~:

Human LINE-1 retrotransposition requires a metastable coiled coil and a positively charged N-terminus in L1ORF1p.,Khazina E, Weichenrieder O Elife. 2018 Mar 22;7. pii: 34960. doi: 10.7554/eLife.34960. PMID:29565245<ref>PMID:29565245</ref>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased Structures~~]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Human]]

[[Category: Khazina, E]]

[[Category: Weichenrieder, O]]

[[Category: Coiled coil]]

[[Category: Genome evolution]]

[[Category: Nucleic acid chaperone]]

[[Category: Retrotransposition]]

[[Category: Rna binding protein]]

[[Category: Rnp]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6fia is ON HOLD
+==Structure of the human LINE-1 ORF1p coiled coil domain==
+<StructureSection load='6fia' size='340' side='right' caption='[[6fia]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6fia]] is a 6 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=6FIA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FIA FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yko|2yko]], [[2ykp|2ykp]], [[2ykq|2ykq]], [[2w7a|2w7a]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">L1RE1, LRE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6fia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fia OCA], [http://pdbe.org/6fia PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fia RCSB], [http://www.ebi.ac.uk/pdbsum/6fia PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fia ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+LINE-1 (L1) is an autonomous retrotransposon, which acted throughout mammalian evolution and keeps contributing to human genotypic diversity, genetic disease and cancer. L1 encodes two essential proteins: L1ORF1p, a unique RNA-binding protein, and L1ORF2p, an endonuclease and reverse transcriptase. L1ORF1p contains an essential, but rapidly evolving N-terminal portion, homo-trimerizes via a coiled coil and packages L1RNA into large assemblies. Here, we determined crystal structures of the entire coiled coil domain of human L1ORF1p. We show that retrotransposition requires a non-ideal and metastable coiled coil structure, and a strongly basic L1ORF1p amino terminus. Human L1ORF1p therefore emerges as a highly calibrated molecular machine, sensitive to mutation but functional in different hosts. Our analysis rationalizes the locally rapid L1ORF1p sequence evolution and reveals striking mechanistic parallels to coiled coil-containing membrane fusion proteins. It also suggests how trimeric L1ORF1p could form larger meshworks and indicates critical novel steps in L1 retrotransposition.
-Authors:
+Human LINE-1 retrotransposition requires a metastable coiled coil and a positively charged N-terminus in L1ORF1p.,Khazina E, Weichenrieder O Elife. 2018 Mar 22;7. pii: 34960. doi: 10.7554/eLife.34960. PMID:29565245<ref>PMID:29565245</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6fia" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Human]]
+[[Category: Khazina, E]]
+[[Category: Weichenrieder, O]]
+[[Category: Coiled coil]]
+[[Category: Genome evolution]]
+[[Category: Nucleic acid chaperone]]
+[[Category: Retrotransposition]]
+[[Category: Rna binding protein]]
+[[Category: Rnp]]