6TC6

Crystal structure of MutM from Neisseria meningitidis

6TC6 の概要

• エントリーDOI: 10.2210/pdb6tc6/pdb
• 分子名称: Formamidopyrimidine-DNA glycosylase, ZINC ION (2 entities in total)
• 機能のキーワード: mutm, fpg/nei, neisseria meningitidis, ber, dna repair, hydrolase
• 由来する生物種: Neisseria meningitidis alpha522
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61936.27

構造登録者

Silhan, J.,Landova, B.,Boura, E. (登録日: 2019-11-05, 公開日: 2020-10-14, 最終更新日: 2024-05-15)

主引用文献

Landova, B.,Silhan, J.
Conformational changes of DNA repair glycosylase MutM triggered by DNA binding.
Febs Lett., 594:3032-3044, 2020

PubMed Abstract: Bacterial MutM is a DNA repair glycosylase removing DNA damage generated from oxidative stress and, therefore, preventing mutations and genomic instability. MutM belongs to the Fpg/Nei family of prokaryotic enzymes sharing structural and functional similarities with their eukaryotic counterparts, for example, NEIL1-NEIL3. Here, we present two crystal structures of MutM from pathogenic Neisseria meningitidis: a MutM holoenzyme and MutM bound to DNA. The free enzyme exists in an open conformation, while upon binding to DNA, both the enzyme and DNA undergo substantial structural changes and domain rearrangement. Our data show that not only NEI glycosylases but also the MutMs undergo dramatic conformational changes. Moreover, crystallographic data support the previously published observations that MutM enzymes are rather flexible and dynamic molecules.

PubMed: 32598485
DOI: 10.1002/1873-3468.13876

実験手法

X-RAY DIFFRACTION (2.9 Å)