4d2i: Difference between revisions
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''' | ==Crystal structure of the HerA hexameric DNA translocase from Sulfolobus solfataricus bound to AMP-PNP== | ||
<StructureSection load='4d2i' size='340' side='right' caption='[[4d2i]], [[Resolution|resolution]] 2.84Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4d2i]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D2I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D2I FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d2i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d2i RCSB], [http://www.ebi.ac.uk/pdbsum/4d2i PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The HerA ATPase cooperates with the NurA nuclease and the Mre11-Rad50 complex for the repair of double-strand DNA breaks in thermophilic archaea. Here we extend our structural knowledge of this minimal end-resection apparatus by presenting the first crystal structure of hexameric HerA. The full-length structure visualizes at atomic resolution the N-terminal HerA-ATP synthase domain and a conserved C-terminal extension, which acts as a physical brace between adjacent protomers. The brace also interacts in trans with nucleotide-binding residues of the neighbouring subunit. Our observations support a model in which the coaxial interaction of the HerA ring with the toroidal NurA dimer generates a continuous channel traversing the complex. HerA-driven translocation would propel the DNA towards the narrow annulus of NurA, leading to duplex melting and nucleolytic digestion. This system differs substantially from the bacterial end-resection paradigms. Our findings suggest a novel mode of DNA-end processing by this integrated archaeal helicase-nuclease machine. | |||
Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea.,Rzechorzek NJ, Blackwood JK, Bray SM, Maman JD, Pellegrini L, Robinson NP Nat Commun. 2014 Nov 25;5:5506. doi: 10.1038/ncomms6506. PMID:25420454<ref>PMID:25420454</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Blackwood, J K]] | |||
[[Category: Bray, S M]] | |||
[[Category: Maman, J D]] | |||
[[Category: Pellegrini, L]] | |||
[[Category: Robinson, N P]] | |||
[[Category: Rzechorzek, N J]] | |||
[[Category: Dna]] | |||
[[Category: Helicase]] | |||
[[Category: Homologous recombination]] | |||
[[Category: Hydrolase]] | |||
[[Category: Mre11]] | |||
[[Category: Nura]] | |||
[[Category: Rad50]] | |||
[[Category: Translocase]] | |||
Revision as of 09:34, 3 December 2014
Crystal structure of the HerA hexameric DNA translocase from Sulfolobus solfataricus bound to AMP-PNP
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