6pr5: Difference between revisions
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<StructureSection load='6pr5' size='340' side='right'caption='[[6pr5]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='6pr5' size='340' side='right'caption='[[6pr5]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6pr5]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PR5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PR5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6pr5]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Corn_earworm_moth Corn earworm moth]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PR5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PR5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6pr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pr5 OCA], [http://pdbe.org/6pr5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pr5 RCSB], [http://www.ebi.ac.uk/pdbsum/6pr5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pr5 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=6pr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pr5 OCA], [http://pdbe.org/6pr5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pr5 RCSB], [http://www.ebi.ac.uk/pdbsum/6pr5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pr5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Transposons have had a pivotal role in genome evolution(1) and are believed to be the evolutionary progenitors of the RAG1-RAG2 recombinase(2), an essential component of the adaptive immune system in jawed vertebrates(3). Here we report one crystal structure and five cryo-electron microscopy structures of Transib(4,5), a RAG1-like transposase from Helicoverpa zea, that capture the entire transposition process from the apo enzyme to the terminal strand transfer complex with transposon ends covalently joined to target DNA, at resolutions of 3.0-4.6 A. These structures reveal a butterfly-shaped complex that undergoes two cycles of marked conformational changes in which the 'wings' of the transposase unfurl to bind substrate DNA, close to execute cleavage, open to release the flanking DNA and close again to capture and attack target DNA. Transib possesses unique structural elements that compensate for the absence of a RAG2 partner, including a loop that interacts with the transposition target site and an accordion-like C-terminal tail that elongates and contracts to help to control the opening and closing of the enzyme and assembly of the active site. Our findings reveal the detailed reaction pathway of a eukaryotic cut-and-paste transposase and illuminate some of the earliest steps in the evolution of the RAG recombinase. | |||
Structures of a RAG-like transposase during cut-and-paste transposition.,Liu C, Yang Y, Schatz DG Nature. 2019 Nov;575(7783):540-544. doi: 10.1038/s41586-019-1753-7. Epub 2019 Nov, 13. PMID:31723264<ref>PMID:31723264</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6pr5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Corn earworm moth]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Liu, C]] | [[Category: Liu, C]] | ||
Revision as of 12:20, 27 November 2019
Cryo-EM structure of HzTransib strand transfer complex (STC)Cryo-EM structure of HzTransib strand transfer complex (STC)
Structural highlights
Publication Abstract from PubMedTransposons have had a pivotal role in genome evolution(1) and are believed to be the evolutionary progenitors of the RAG1-RAG2 recombinase(2), an essential component of the adaptive immune system in jawed vertebrates(3). Here we report one crystal structure and five cryo-electron microscopy structures of Transib(4,5), a RAG1-like transposase from Helicoverpa zea, that capture the entire transposition process from the apo enzyme to the terminal strand transfer complex with transposon ends covalently joined to target DNA, at resolutions of 3.0-4.6 A. These structures reveal a butterfly-shaped complex that undergoes two cycles of marked conformational changes in which the 'wings' of the transposase unfurl to bind substrate DNA, close to execute cleavage, open to release the flanking DNA and close again to capture and attack target DNA. Transib possesses unique structural elements that compensate for the absence of a RAG2 partner, including a loop that interacts with the transposition target site and an accordion-like C-terminal tail that elongates and contracts to help to control the opening and closing of the enzyme and assembly of the active site. Our findings reveal the detailed reaction pathway of a eukaryotic cut-and-paste transposase and illuminate some of the earliest steps in the evolution of the RAG recombinase. Structures of a RAG-like transposase during cut-and-paste transposition.,Liu C, Yang Y, Schatz DG Nature. 2019 Nov;575(7783):540-544. doi: 10.1038/s41586-019-1753-7. Epub 2019 Nov, 13. PMID:31723264[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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