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5bq5

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'''Unreleased structure'''
 
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The entry 5bq5 is ON HOLD
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==Crystal structure of the IstB AAA+ domain bound to ADP-BeF3==
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<StructureSection load='5bq5' size='340' side='right'caption='[[5bq5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5bq5]] is a 3 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=5BQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BQ5 FirstGlance]. <br>
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</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=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5bq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bq5 OCA], [https://pdbe.org/5bq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bq5 RCSB], [https://www.ebi.ac.uk/pdbsum/5bq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bq5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ISTB_GEOSE ISTB_GEOSE]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Transposons are ubiquitous genetic elements that drive genome rearrangements, evolution, and the spread of infectious disease and drug-resistance. Many transposons, such as Mu, Tn7, and IS21, require regulatory AAA+ ATPases for function. We use X-ray crystallography and cryo-electron microscopy to show that the ATPase subunit of IS21, IstB, assembles into a clamshell-shaped decamer that sandwiches DNA between two helical pentamers of ATP-associated AAA+ domains, sharply bending the duplex into a 180 degrees U-turn. Biochemical studies corroborate key features of the structure and further show that the IS21 transposase, IstA, recognizes the IstB*DNA complex and promotes its disassembly by stimulating ATP hydrolysis. Collectively, these studies reveal a distinct manner of higher-order assembly and client engagement by a AAA+ ATPase and suggest a mechanistic model where IstB binding and subsequent DNA bending primes a selected insertion site for efficient transposition.
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Authors: Arias-Palomo, E., Berger, J.M.
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An Atypical AAA+ ATPase Assembly Controls Efficient Transposition through DNA Remodeling and Transposase Recruitment.,Arias-Palomo E, Berger JM Cell. 2015 Aug 13;162(4):860-71. doi: 10.1016/j.cell.2015.07.037. PMID:26276634<ref>PMID:26276634</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Arias-Palomo, E]]
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<div class="pdbe-citations 5bq5" style="background-color:#fffaf0;"></div>
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[[Category: Berger, J.M]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Geobacillus stearothermophilus]]
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[[Category: Large Structures]]
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[[Category: Arias-Palomo E]]
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[[Category: Berger JM]]

Current revision

Crystal structure of the IstB AAA+ domain bound to ADP-BeF3

PDB ID 5bq5

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