6ZPC

Cyanophage S-2L HD phosphohydrolase (DatZ) bound to dATP

6ZPC の概要

• エントリーDOI: 10.2210/pdb6zpc/pdb
• 分子名称: DatZ, 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE, ZINC ION, ... (5 entities in total)
• 機能のキーワード: s-2l, hd phosphohydrolase, datz, viral protein
• 由来する生物種: Cyanophage S-2L
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21183.08

構造登録者

Czernecki, D.,Legrand, P.,Delarue, M. (登録日: 2020-07-08, 公開日: 2021-03-03, 最終更新日: 2024-05-15)

主引用文献

Czernecki, D.,Legrand, P.,Tekpinar, M.,Rosario, S.,Kaminski, P.A.,Delarue, M.
How cyanophage S-2L rejects adenine and incorporates 2-aminoadenine to saturate hydrogen bonding in its DNA.
Nat Commun, 12:2420-2420, 2021

PubMed Abstract: Bacteriophages have long been known to use modified bases in their DNA to prevent cleavage by the host's restriction endonucleases. Among them, cyanophage S-2L is unique because its genome has all its adenines (A) systematically replaced by 2-aminoadenines (Z). Here, we identify a member of the PrimPol family as the sole possible polymerase of S-2L and we find it can incorporate both A and Z in front of a T. Its crystal structure at 1.5 Å resolution confirms that there is no structural element in the active site that could lead to the rejection of A in front of T. To resolve this contradiction, we show that a nearby gene is a triphosphohydolase specific of dATP (DatZ), that leaves intact all other dNTPs, including dZTP. This explains the absence of A in S-2L genome. Crystal structures of DatZ with various ligands, including one at sub-angstrom resolution, allow to describe its mechanism as a typical two-metal-ion mechanism and to set the stage for its engineering.

PubMed: 33893297
DOI: 10.1038/s41467-021-22626-x

実験手法

X-RAY DIFFRACTION (1.26835935206 Å)