6FKE

Structure of 3' phosphatase NExo (D146N) from Neisseria bound to product DNA hairpin

6FKE の概要

• エントリーDOI: 10.2210/pdb6fke/pdb
• 関連するPDBエントリー: 6FK4 6FK5
• 分子名称: Exodeoxyribonuclease III, DNA (5'-D(*GP*TP*AP*GP*CP*GP*AP*AP*GP*CP*TP*A)-3'), (4S)-2-METHYL-2,4-PENTANEDIOL, ... (5 entities in total)
• 機能のキーワード: 3' phosphatase, base excision dna repair., dna binding protein
• 由来する生物種: Neisseria meningitidis MC58; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34203.54

構造登録者

Silhan, J.,Zhao, Q.,Boura, E.,Thomson, H.,Foster, A.,Tang, C.M.,Freemont, P.S.,Baldwin, G.S. (登録日: 2018-01-23, 公開日: 2018-10-31, 最終更新日: 2024-01-17)

主引用文献

Silhan, J.,Zhao, Q.,Boura, E.,Thomson, H.,Forster, A.,Tang, C.M.,Freemont, P.S.,Baldwin, G.S.
Structural basis for recognition and repair of the 3'-phosphate by NExo, a base excision DNA repair nuclease from Neisseria meningitidis.
Nucleic Acids Res., 46:11980-11989, 2018

PubMed Abstract: NExo is an enzyme from Neisseria meningitidis that is specialized in the removal of the 3'-phosphate and other 3'-lesions, which are potential blocks for DNA repair. NExo is a highly active DNA 3'-phosphatase, and although it is from the class II AP family it lacks AP endonuclease activity. In contrast, the NExo homologue NApe, lacks 3'-phosphatase activity but is an efficient AP endonuclease. These enzymes act together to protect the meningococcus from DNA damage arising mainly from oxidative stress and spontaneous base loss. In this work, we present crystal structures of the specialized 3'-phosphatase NExo bound to DNA in the presence and absence of a 3'-phosphate lesion. We have outlined the reaction mechanism of NExo, and using point mutations we bring mechanistic insights into the specificity of the 3'-phosphatase activity of NExo. Our data provide further insight into the molecular origins of plasticity in substrate recognition for this class of enzymes. From this we hypothesize that these specialized enzymes lead to enhanced efficiency and accuracy of DNA repair and that this is important for the biological niche occupied by this bacterium.

PubMed: 30329088
DOI: 10.1093/nar/gky934

実験手法

X-RAY DIFFRACTION (2.151 Å)