4OT0

Crystal structure of the S505T mutant of TAL effector dHax3

4OT0 の概要

• エントリーDOI: 10.2210/pdb4ot0/pdb
• 関連するPDBエントリー: 4OSH 4OSI 4OSJ 4OSK 4OSL 4OSM 4OSQ 4OSR 4OSS 4OST 4OSV 4OSW 4OSZ 4OT3 4OTO
• 分子名称: Hax3, DNA (5'-D(*TP*GP*TP*CP*CP*CP*TP*TP*TP*AP*TP*CP*TP*CP*TP*CP*T)-3'), DNA (5'-D(*AP*GP*AP*GP*AP*GP*AP*TP*AP*AP*AP*GP*GP*GP*AP*CP*A)-3'), ... (4 entities in total)
• 機能のキーワード: dna binding protein, dna, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Xanthomonas campestris pv. armoraciae
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 124362.65

構造登録者

Deng, D.,Wu, J.P.,Yan, C.Y.,Pan, X.J.,Yan, N. (登録日: 2014-02-13, 公開日: 2014-05-28, 最終更新日: 2023-11-08)

主引用文献

Deng, D.,Yan, C.Y.,Wu, J.P.,Pan, X.J.,Yan, N.
Revisiting the TALE repeat
Protein Cell, 5:297-306, 2014

PubMed Abstract: Transcription activator-like (TAL) effectors specifically bind to double stranded (ds) DNA through a central domain of tandem repeats. Each TAL effector (TALE) repeat comprises 33-35 amino acids and recognizes one specific DNA base through a highly variable residue at a fixed position in the repeat. Structural studies have revealed the molecular basis of DNA recognition by TALE repeats. Examination of the overall structure reveals that the basic building block of TALE protein, namely a helical hairpin, is one-helix shifted from the previously defined TALE motif. Here we wish to suggest a structure-based re-demarcation of the TALE repeat which starts with the residues that bind to the DNA backbone phosphate and concludes with the base-recognition hyper-variable residue. This new numbering system is consistent with the α-solenoid superfamily to which TALE belongs, and reflects the structural integrity of TAL effectors. In addition, it confers integral number of TALE repeats that matches the number of bound DNA bases. We then present fifteen crystal structures of engineered dHax3 variants in complex with target DNA molecules, which elucidate the structural basis for the recognition of bases adenine (A) and guanine (G) by reported or uncharacterized TALE codes. Finally, we analyzed the sequence-structure correlation of the amino acid residues within a TALE repeat. The structural analyses reported here may advance the mechanistic understanding of TALE proteins and facilitate the design of TALEN with improved affinity and specificity.

PubMed: 24622844
DOI: 10.1007/s13238-014-0035-2

実験手法

X-RAY DIFFRACTION (2.491 Å)