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4B6G

The Crystal Structure of the Neisserial Esterase D.

4B6G の概要
エントリーDOI10.2210/pdb4b6g/pdb
分子名称PUTATIVE ESTERASE (2 entities in total)
機能のキーワードhydrolase, formaldehyde detoxification, alpha/beta serine hydrolase
由来する生物種NEISSERIA MENINGITIDIS MC58
タンパク質・核酸の鎖数2
化学式量合計64776.39
構造登録者
Counago, R.M.,Kobe, B. (登録日: 2012-08-13, 公開日: 2012-11-14, 最終更新日: 2023-12-20)
主引用文献Chen, N.H.,Counago, R.M.,Djoko, K.Y.,Jennings, M.P.,Apicella, M.A.,Kobe, B.,McEwan, A.G.
A glutathione-dependent detoxification system is required for formaldehyde resistance and optimal survival of Neisseria meningitidis in biofilms.
Antioxid. Redox Signal., 18:743-755, 2013
Cited by
PubMed Abstract: The glutathione-dependent AdhC-EstD formaldehyde detoxification system is found in eukaryotes and prokaryotes. It is established that it confers protection against formaldehyde that is produced from environmental sources or methanol metabolism. Thus, its presence in the human host-adapted bacterial pathogen Neisseria meningitidis is intriguing. This work defined the biological function of this system in the meningococcus using phenotypic analyses of mutants linked to biochemical and structural characterization of purified enzymes.
PubMed: 22937752
DOI: 10.1089/ars.2012.4749
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.4 Å)
構造検証レポート
Validation report summary of 4b6g
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-23に公開中

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