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4GG4

Crystal structure of the TAL effector dHax3 bound to specific DNA-RNA hybrid

Summary for 4GG4
Entry DOI10.2210/pdb4gg4/pdb
Related3V6P 3V6T
DescriptorHax3, DNA (5'-D(*TP*GP*TP*CP*CP*CP*TP*TP*TP*AP*TP*CP*TP*CP*TP*CP*T)-3'), RNA (5'-R(*AP*GP*AP*GP*AP*GP*AP*UP*AP*AP*AP*GP*GP*GP*AP*CP*A)-3'), ... (4 entities in total)
Functional Keywordstandem repeat, tal effector, sequence specific dna binding protein, dna duplex, dna-rna hybrid, dna binding protein-dna-rna complex, dna binding protein/dna/rna
Biological sourceXanthomonas campestris pv. armoraciae
More
Total number of polymer chains3
Total formula weight62451.35
Authors
Yin, P.,Deng, D.,Yan, C.Y.,Pan, X.J.,Yan, N.,Shi, Y.G. (deposition date: 2012-08-05, release date: 2012-10-03, Last modification date: 2023-11-08)
Primary citationYin, P.,Deng, D.,Yan, C.,Pan, X.J.,Xi, J.J.,Yan, N.,Shi, Y.
Specific DNA-RNA hybrid recognition by TAL effectors
Cell Rep, 2:707-713, 2012
Cited by
PubMed Abstract: The transcription activator-like (TAL) effector targets specific host promoter through its central DNA-binding domain, which comprises multiple tandem repeats (TALE repeats). Recent structural analyses revealed that the TALE repeats form a superhelical structure that tracks along the forward strand of the DNA duplex. Here, we demonstrate that TALE repeats specifically recognize a DNA-RNA hybrid where the DNA strand determines the binding specificity. The crystal structure of a designed TALE in complex with the DNA-RNA hybrid was determined at a resolution of 2.5 Å. Although TALE repeats are in direct contact with only the DNA strand, the phosphodiester backbone of the RNA strand is inaccessible by macromolecules such as RNases. Consistent with this observation, sequence-specific recognition of an HIV-derived DNA-RNA hybrid by an engineered TALE efficiently blocked RNase H-mediated degradation of the RNA strand. Our study broadens the utility of TALE repeats and suggests potential applications in processes involving DNA replication and retroviral infections.
PubMed: 23022487
DOI: 10.1016/j.celrep.2012.09.001
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.501 Å)
Structure validation

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