5f55: Difference between revisions
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<StructureSection load='5f55' size='340' side='right'caption='[[5f55]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='5f55' size='340' side='right'caption='[[5f55]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5f55]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5f55]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F55 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5f55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f55 OCA], [https://pdbe.org/5f55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f55 RCSB], [https://www.ebi.ac.uk/pdbsum/5f55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f55 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/D0EM60_DEIRD D0EM60_DEIRD] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Deinococcus radiodurans]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Cheng K]] | ||
[[Category: | [[Category: Hua Y]] | ||
[[Category: | [[Category: Zhao Y]] | ||
Latest revision as of 11:47, 12 July 2023
Structure of RecJ complexed with DNAStructure of RecJ complexed with DNA
Structural highlights
FunctionPublication Abstract from PubMedThe resection of DNA strand with a 5 end at double-strand breaks is an essential step in recombinational DNA repair. RecJ, a member of DHH family proteins, is the only 5 nuclease involved in the RecF recombination pathway. Here, we report the crystal structures of Deinococcus radiodurans RecJ in complex with deoxythymidine monophosphate (dTMP), ssDNA, the C-terminal region of single-stranded DNA-binding protein (SSB-Ct) and a mechanistic insight into the RecF pathway. A terminal 5 -phosphate-binding pocket above the active site determines the 5 -3 polarity of the deoxy-exonuclease of RecJ; a helical gateway at the entrance to the active site admits ssDNA only; and the continuous stacking interactions between protein and nine nucleotides ensure the processive end resection. The active site of RecJ in the N-terminal domain contains two divalent cations that coordinate the nucleophilic water. The ssDNA makes a 180 degrees turn at the scissile phosphate. The C-terminal domain of RecJ binds the SSB-Ct, which explains how RecJ and SSB work together to efficiently process broken DNA ends for homologous recombination. Structural basis for DNA 5 -end resection by RecJ.,Cheng K, Xu H, Chen X, Wang L, Tian B, Zhao Y, Hua Y Elife. 2016 Apr 8;5. pii: e14294. doi: 10.7554/eLife.14294. PMID:27058167[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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