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4L8L

Crystal Structure of the Type II Dehydroquinase from Pseudomonas aeruginosa

4L8L の概要
エントリーDOI10.2210/pdb4l8l/pdb
分子名称3-dehydroquinate dehydratase 1 (2 entities in total)
機能のキーワードflavodoxin-like fold, rossmann fold, alpha helix, beta sheet, dehydratase, dehydroquinic acid, lyase
由来する生物種Pseudomonas aeruginosa
タンパク質・核酸の鎖数1
化学式量合計15985.02
構造登録者
Reiling, S.A.,Asojo, O.A. (登録日: 2013-06-17, 公開日: 2014-07-23, 最終更新日: 2024-02-28)
主引用文献Reiling, S.,Kelleher, A.,Matsumoto, M.M.,Robinson, G.,Asojo, O.A.
Structure of type II dehydroquinase from Pseudomonas aeruginosa.
Acta Crystallogr F Struct Biol Commun, 70:1485-1491, 2014
Cited by
PubMed Abstract: Pseudomonas aeruginosa causes opportunistic infections and is resistant to most antibiotics. Ongoing efforts to generate much-needed new antibiotics include targeting enzymes that are vital for P. aeruginosa but are absent in mammals. One such enzyme, type II dehydroquinase (DHQase), catalyzes the interconversion of 3-dehydroquinate and 3-dehydroshikimate, a necessary step in the shikimate pathway. This step is vital for the proper synthesis of phenylalanine, tryptophan, tyrosine and other aromatic metabolites. The recombinant expression, purification and crystal structure of catalytically active DHQase from P. aeruginosa (PaDHQase) are presented. Cubic crystals belonging to space group F23, with unit-cell parameters a=b=c=125.39 Å, were obtained by vapor diffusion in sitting drops and the structure was refined to an R factor of 16% at 1.74 Å resolution. PaDHQase is a prototypical type II DHQase with the classical flavodoxin-like α/β topology.
PubMed: 25372814
DOI: 10.1107/S2053230X14020214
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.74 Å)
構造検証レポート
Validation report summary of 4l8l
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2026-04-29に公開中

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