6IOB

The structure of the H109A mutant of UdgX in complex with uracil

6IOB の概要

• エントリーDOI: 10.2210/pdb6iob/pdb
• 分子名称: Phage SPO1 DNA polymerase-related protein, URACIL, IRON/SULFUR CLUSTER, ... (4 entities in total)
• 機能のキーワード: uracil dna glycosylase, dna repair, iron-sulfur, dna binding protein
• 由来する生物種: Mycolicibacterium smegmatis MC2 155
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22880.22

構造登録者

Xie, W.,Tu, J. (登録日: 2018-10-29, 公開日: 2019-07-24, 最終更新日: 2024-03-27)

主引用文献

Tu, J.,Chen, R.,Yang, Y.,Cao, W.,Xie, W.
Suicide inactivation of the uracil DNA glycosylase UdgX by covalent complex formation.
Nat.Chem.Biol., 15:615-622, 2019

PubMed Abstract: A uracil DNA glycosylase (UDG) from Mycobacterium smegmatis (MsmUdgX) shares sequence similarity with family 4 UDGs and forms exceedingly stable complexes with single-stranded uracil-containing DNAs (ssDNA-Us) that are resistant to denaturants. However, MsmUdgX has been reported to be inactive in excising uracil from ssDNA-Us and the underlying structural basis is unclear. Here, we report high-resolution crystal structures of MsmUdgX in the free, uracil- and DNA-bound forms, respectively. The structural information, supported by mutational and biochemical analyses, indicates that the conserved residue His109 located on a characteristic loop forms an irreversible covalent linkage with the deoxyribose at the apyrimidinic site of ssDNA-U, thus rendering the enzyme unable to regenerate. By proposing the catalytic pathway and molecular mechanism for MsmUdgX, our studies provide an insight into family 4 UDGs and UDGs in general.

PubMed: 31101915
DOI: 10.1038/s41589-019-0290-x

実験手法

X-RAY DIFFRACTION (2.002 Å)