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5F55

Structure of RecJ complexed with DNA

Summary for 5F55
Entry DOI10.2210/pdb5f55/pdb
Related5F54 5F56
DescriptorSingle-stranded-DNA-specific exonuclease, DNA (5'-D(*GP*AP*TP*GP*TP*AP*CP*GP*CP*TP*AP*GP*GP*C)-3'), SULFATE ION, ... (4 entities in total)
Functional Keywordsrecf pathway, dna end resection, two-metal-ion catalysis, single-strand-dna, dna binding protein-dna complex, dna binding protein/dna
Biological sourceDeinococcus radiodurans
More
Total number of polymer chains2
Total formula weight81134.67
Authors
Hua, Y.,Zhao, Y.,Cheng, K. (deposition date: 2015-12-04, release date: 2016-06-15, Last modification date: 2023-11-08)
Primary citationCheng, K.,Xu, H.,Chen, X.,Wang, L.,Tian, B.,Zhao, Y.,Hua, Y.
Structural basis for DNA 5 -end resection by RecJ
Elife, 5:e14294-e14294, 2016
Cited by
PubMed Abstract: The 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° 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.
PubMed: 27058167
DOI: 10.7554/eLife.14294
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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