6FL4

A. thaliana NUDT1 in complex with 8-oxo-dGTP

6FL4 の概要

• エントリーDOI: 10.2210/pdb6fl4/pdb
• 分子名称: Nudix hydrolase 1, MAGNESIUM ION, 8-OXO-2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: 8-oxo-dgtp, hydrolase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33890.69

構造登録者

Jemth, A.S.,Scaletti-Hutchinson, E.,Carter, M.,Helleday, T.,Stenmark, P. (登録日: 2018-01-25, 公開日: 2019-02-06, 最終更新日: 2024-05-08)

主引用文献

Jemth, A.S.,Scaletti, E.,Carter, M.,Helleday, T.,Stenmark, P.
Crystal Structure and Substrate Specificity of the 8-oxo-dGTP Hydrolase NUDT1 from Arabidopsis thaliana.
Biochemistry, 58:887-899, 2019

PubMed Abstract: Arabidopsis thaliana NUDT1 (AtNUDT1) belongs to the Nudix family of proteins, which have a diverse range of substrates, including oxidized nucleotides such as 8-oxo-dGTP. The hydrolysis of oxidized dNTPs is highly important as it prevents their incorporation into DNA, thus preventing mutations and DNA damage. AtNUDT1 is the sole Nudix enzyme from A. thaliana shown to have activity against 8-oxo-dGTP. We present the structure of AtNUDT1 in complex with 8-oxo-dGTP. Structural comparison with bacterial and human homologues reveals a conserved overall fold. Analysis of the 8-oxo-dGTP binding mode shows that the residues Asn76 and Ser89 interact with the O8 atom of the substrate, a feature not observed in structures of protein homologues solved to date. Kinetic analysis of wild-type and mutant AtNUDT1 confirmed that these active site residues influence 8-oxo-dGTP hydrolysis. A recent study showed that AtNUDT1 is also able to hydrolyze terpene compounds. The diversity of reactions catalyzed by AtNUDT1 suggests that this Nudix enzyme from higher plants has evolved in a manner distinct to those from other organisms.

PubMed: 30614695
DOI: 10.1021/acs.biochem.8b00950

実験手法

X-RAY DIFFRACTION (1.6 Å)