5bq5
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Crystal structure of the IstB AAA+ domain bound to ADP-BeF3== |
| + | <StructureSection load='5bq5' size='340' side='right' caption='[[5bq5]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5bq5]] is a 3 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BQ5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5bq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bq5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5bq5 RCSB], [http://www.ebi.ac.uk/pdbsum/5bq5 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Arias-Palomo, E]] | [[Category: Arias-Palomo, E]] | ||
| - | [[Category: Berger, J | + | [[Category: Berger, J M]] |
| + | [[Category: Aaa+]] | ||
| + | [[Category: Atp-binding protein]] | ||
| + | [[Category: Atpase]] | ||
| + | [[Category: Dna binding]] | ||
| + | [[Category: Transposition]] | ||
Revision as of 12:27, 2 September 2015
Crystal structure of the IstB AAA+ domain bound to ADP-BeF3
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