7f6d
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<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> | <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> | ||
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.85Å</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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/Q9RW33_DEIRA Q9RW33_DEIRA] | |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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. | 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. | ||
| - | 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 | + | 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 Sep 1;30(9):1298-1306.e3. doi: 10.1016/j.str.2022.06.005. Epub , 2022 Jul 15. PMID:35841886<ref>PMID:35841886</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
Reconstruction of the HerA-NurA complex from Deinococcus radiodurans
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Categories: Deinococcus radiodurans R1 | Large Structures | Guo J | Hua Y | Xu L | Xu Y | Zhao Y
