8q4d: Difference between revisions

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'''Unreleased structure'''


The entry 8q4d is ON HOLD
==IstA-IstB(E167Q) Strand Transfer Complex==
<StructureSection load='8q4d' size='340' side='right'caption='[[8q4d]], [[Resolution|resolution]] 3.62&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8q4d]] is a 30 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8Q4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8Q4D FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.62&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=8q4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8q4d OCA], [https://pdbe.org/8q4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8q4d RCSB], [https://www.ebi.ac.uk/pdbsum/8q4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8q4d ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRA6_GEOSE TRA6_GEOSE] Involved in the transposition of the insertion sequence.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Transposases drive chromosomal rearrangements and the dissemination of drug-resistance genes and toxins(1-3). Although some transposases act alone, many rely on dedicated AAA+ ATPase subunits that regulate site selectivity and catalytic function through poorly understood mechanisms. Using IS21 as a model transposase system, we show how an ATPase regulator uses nucleotide-controlled assembly and DNA deformation to enable structure-based site selectivity, transposase recruitment, and activation and integration. Solution and cryogenic electron microscopy studies show that the IstB ATPase self-assembles into an autoinhibited pentamer of dimers that tightly curves target DNA into a half-coil. Two of these decamers dimerize, which stabilizes the target nucleic acid into a kinked S-shaped configuration that engages the IstA transposase at the interface between the two IstB oligomers to form an approximately 1 MDa transpososome complex. Specific interactions stimulate regulator ATPase activity and trigger a large conformational change on the transposase that positions the catalytic site to perform DNA strand transfer. These studies help explain how AAA+ ATPase regulators-which are used by classical transposition systems such as Tn7, Mu and CRISPR-associated elements-can remodel their substrate DNA and cognate transposases to promote function.


Authors:  
Molecular basis for transposase activation by a dedicated AAA+ ATPase.,de la Gandara A, Spinola-Amilibia M, Araujo-Bazan L, Nunez-Ramirez R, Berger JM, Arias-Palomo E Nature. 2024 Jun;630(8018):1003-1011. doi: 10.1038/s41586-024-07550-6. Epub 2024 , Jun 26. PMID:38926614<ref>PMID:38926614</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 8q4d" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Geobacillus stearothermophilus]]
[[Category: Large Structures]]
[[Category: Araujo-Bazan L]]
[[Category: Arias-Palomo E]]
[[Category: Berger JM]]
[[Category: Nunez-Ramirez R]]
[[Category: Spinola-Amilibia M]]
[[Category: De la Gandara A]]
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