4B5M

Neisseria AP endonuclease bound to the substrate with a cytosine orphan base

4B5M の概要

• エントリーDOI: 10.2210/pdb4b5m/pdb
• 関連するPDBエントリー: 4B5F 4B5G 4B5H 4B5I 4B5J
• 分子名称: PUTATIVE EXODEOXYRIBONUCLEASE, 5'-D(*3DRP*CP*AP*TP*CP*GP)-3', 5'-D(*GP*CP*TP*AP*CP)-3', ... (4 entities in total)
• 機能のキーワード: hydrolase-dna complex, hydrolase/dna
• 由来する生物種: NEISSERIA MENINGITIDIS; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 108641.77

構造登録者

Lu, D.,Silhan, J.,MacDonald, J.T.,Carpenter, E.P.,Jensen, K.,Tang, C.M.,Baldwin, G.S.,Freemont, P.S. (登録日: 2012-08-06, 公開日: 2012-10-17, 最終更新日: 2024-05-08)

主引用文献

Lu, D.,Silhan, J.,MacDonald, J.T.,Carpenter, E.P.,Jensen, K.,Tang, C.M.,Baldwin, G.S.,Freemont, P.S.
Structural basis for the recognition and cleavage of abasic DNA in Neisseria meningitidis.
Proc. Natl. Acad. Sci. U.S.A., 109:16852-16857, 2012

PubMed Abstract: Base excision repair (BER) is a highly conserved DNA repair pathway throughout all kingdoms from bacteria to humans. Whereas several enzymes are required to complete the multistep repair process of damaged bases, apurinic-apyrimidic (AP) endonucleases play an essential role in enabling the repair process by recognizing intermediary abasic sites cleaving the phosphodiester backbone 5' to the abasic site. Despite extensive study, there is no structure of a bacterial AP endonuclease bound to substrate DNA. Furthermore, the structural mechanism for AP-site cleavage is incomplete. Here we report a detailed structural and biochemical study of the AP endonuclease from Neisseria meningitidis that has allowed us to capture structural intermediates providing more complete snapshots of the catalytic mechanism. Our data reveal subtle differences in AP-site recognition and kinetics between the human and bacterial enzymes that may reflect different evolutionary pressures.

PubMed: 23035246
DOI: 10.1073/pnas.1206563109

実験手法

X-RAY DIFFRACTION (2.758 Å)