5F54

Structure of RecJ complexed with dTMP

Summary for 5F54

• Entry DOI: 10.2210/pdb5f54/pdb
• Related: 5F55 5F56
• Descriptor: Single-stranded-DNA-specific exonuclease, MANGANESE (II) ION, THYMIDINE-5'-PHOSPHATE, ... (4 entities in total)
• Functional Keywords: recf pathway, dna end resection, two-metal-ion catalysis, single-strand-dna, dna binding protein
• Biological source: Deinococcus radiodurans
• Total number of polymer chains: 1
• Total formula weight: 76463.62

Authors

Hua, Y.,Zhao, Y.,Cheng, K. (deposition date: 2015-12-04, release date: 2016-06-15, Last modification date: 2023-11-08)

Primary citation

Cheng, 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

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

Experimental method

X-RAY DIFFRACTION (2.7 Å)