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7f6d

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(New page: '''Unreleased structure''' The entry 7f6d is ON HOLD Authors: Description: Category: Unreleased Structures)
Current revision (07:01, 14 September 2022) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 7f6d is ON HOLD
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==Reconstruction of the HerA-NurA complex from Deinococcus radiodurans==
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<StructureSection load='7f6d' size='340' side='right'caption='[[7f6d]], [[Resolution|resolution]] 3.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7f6d]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7F6D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F6D FirstGlance]. <br>
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</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=7f6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f6d OCA], [https://pdbe.org/7f6d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f6d RCSB], [https://www.ebi.ac.uk/pdbsum/7f6d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f6d ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/Q9RW33_DEIRA Q9RW33_DEIRA]]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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DNA end resection mediated by the coordinated action of nuclease and helicase is a crucial step in initiating homologous recombination. The end-resection apparatus NurA nuclease and HerA helicase are present in both archaea and bacteria. Here, we report the cryo-electron microscopy structure of a bacterial HerA-NurA complex from Deinococcus radiodurans. The structure reveals a barrel-like hexameric HerA and a distinctive NurA dimer subcomplex, which has a unique extended N-terminal region (ENR) involved in bacterial NurA dimerization and activation. In addition to the long protruding linking loop and the C-terminal alpha helix of NurA, the flexible ENR is close to the HerA-NurA interface and divides the central channel of the DrNurA dimer into two halves, suggesting a possible mechanism of DNA end processing. In summary, this work provides new insights into the structure, assembly, and activation mechanisms of bacterial DNA end resection mediated by a minimal end-resection apparatus.
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Authors:
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Mechanisms of helicase activated DNA end resection in bacteria.,Xu Y, Xu L, Qin C, Wang L, Guo J, Hua Y, Zhao Y Structure. 2022 Jul 5. pii: S0969-2126(22)00236-2. doi:, 10.1016/j.str.2022.06.005. PMID:35841886<ref>PMID:35841886</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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<div class="pdbe-citations 7f6d" style="background-color:#fffaf0;"></div>
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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: Deinococcus radiodurans R1]]
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[[Category: Large Structures]]
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[[Category: Guo J]]
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[[Category: Hua Y]]
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[[Category: Xu L]]
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[[Category: Xu Y]]
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[[Category: Zhao Y]]

Current revision

Reconstruction of the HerA-NurA complex from Deinococcus radiodurans

PDB ID 7f6d

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