4ol8
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ol8]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OL8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ol8]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OL8 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3.1Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4ol8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ol8 OCA], [https://pdbe.org/4ol8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ol8 RCSB], [https://www.ebi.ac.uk/pdbsum/4ol8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ol8 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=4ol8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ol8 OCA], [https://pdbe.org/4ol8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ol8 RCSB], [https://www.ebi.ac.uk/pdbsum/4ol8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ol8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Function == | ||
| - | [https://www.uniprot.org/uniprot/YG31B_YEAST YG31B_YEAST] Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the genomic RNA-nucleocapsid complex.<ref>PMID:2159534</ref> <ref>PMID:1371165</ref> <ref>PMID:7515969</ref> <ref>PMID:10593967</ref> Nucleocapsid protein p11 (NC) forms the nucleocore that coats the retro-elements dimeric RNA. Binds these RNAs through its zinc fingers (By similarity). Promotes primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty3 RNA and initiation of reverse transcription.<ref>PMID:2159534</ref> <ref>PMID:1371165</ref> <ref>PMID:7515969</ref> <ref>PMID:10593967</ref> The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP.<ref>PMID:2159534</ref> <ref>PMID:1371165</ref> <ref>PMID:7515969</ref> <ref>PMID:10593967</ref> Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends.<ref>PMID:2159534</ref> <ref>PMID:1371165</ref> <ref>PMID:7515969</ref> <ref>PMID:10593967</ref> Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome.<ref>PMID:2159534</ref> <ref>PMID:1371165</ref> <ref>PMID:7515969</ref> <ref>PMID:10593967</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Current revision
Ty3 reverse transcriptase bound to DNA/RNA
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