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4S1H

Pyridoxal kinase of Entamoeba histolytica with ADP

4S1H の概要
エントリーDOI10.2210/pdb4s1h/pdb
関連するPDBエントリー4S1I
分子名称Pyridoxal kinase, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
機能のキーワードpyridoxal 5'-phosphate, transferase
由来する生物種Entamoeba histolytica
タンパク質・核酸の鎖数2
化学式量合計65143.54
構造登録者
Tarique, K.F.,Devi, S.,Abdul Rehman, S.A.,Gourinath, S. (登録日: 2015-01-13, 公開日: 2015-01-28, 最終更新日: 2024-04-03)
主引用文献Tarique, K.F.,Devi, S.,Tomar, P.,Ali, M.F.,Rehman, S.A.A.,Gourinath, S.
Characterization and functional insights into the Entamoeba histolytica pyridoxal kinase, an enzyme essential for its survival.
J.Struct.Biol., 212:107645-107645, 2020
Cited by
PubMed Abstract: Pyridoxal 5'-phosphate (PLP) is the active form of vitamin B and a cofactor for more than 140 enzymes. This coenzyme plays a pivotal role in catalysis of various enzymatic reactions that are critical for the survival of organisms. Entamoeba histolytica depends on the uptake of pyridoxal (PL), a B vitamer from the external environment which is then phosphorylated by pyridoxal kinase (EhPLK) to form PLP via the salvage pathway. E. histolytica cannot synthesise vitamin Bde-novo, and also lacks pyridoxine 5'-phosphate oxidase, a salvage pathway enzyme required to produce PLP from pyridoxine phosphate (PNP) and pyridoxamine phosphate (PMP). Analysing the importance of PLK in E. histolytica, we have determined the high-resolution crystal structures of the dimeric pyridoxal kinase in apo, ADP-bound, and PLP-bound states. These structures provided a snapshot of the transition state and help in understanding the reaction mechanism in greater detail. The EhPLK structure significantly differed from the human homologue at its PLP binding site, and the phylogenetic study also revealed its divergence from human PLK. Further, gene regulation of EhPLK using sense and antisense RNA showed that any change in optimal level is harmful to the pathogen. Biochemical and in vivo studies unveiled EhPLK to be essential for this pathogen, while the molecular differences with human PLK structure can be exploited for the structure-guided design of EhPLK inhibitors.
PubMed: 33045383
DOI: 10.1016/j.jsb.2020.107645
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.6 Å)
構造検証レポート
Validation report summary of 4s1h
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2024-10-30に公開中

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