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6AA9

T166A mutant of D-Serine deaminase from Salmonella typhimurium

6AA9 の概要
エントリーDOI10.2210/pdb6aa9/pdb
分子名称D-serine dehydratase, SODIUM ION, PHOSPHATE ION, ... (4 entities in total)
機能のキーワードmonomer, plp bound, salmonella typhimurium, deaminase, lyase
由来する生物種Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
タンパク質・核酸の鎖数1
化学式量合計48802.93
構造登録者
Deka, G.,Bharath, S.R.,Shavithri, H.S.,Murthy, M.R.N. (登録日: 2018-07-17, 公開日: 2019-07-17, 最終更新日: 2023-11-22)
主引用文献Deka, G.,Bharath, S.R.,Shavithri, H.S.,Murthy, M.R.N.
Structural studies on the decameric S. typhimurium arginine decarboxylase (ADC): Pyridoxal 5'-phosphate binding induces conformational changes
Biochem. Biophys. Res. Commun., 490:1362-1368, 2017
Cited by
PubMed Abstract: Enteric pathogens such as Salmonella typhimurium colonize the human gut in spite of the lethal acidic pH environment (pH < 2.5) due to the activation of inducible acid tolerance response (ATR) systems. The pyridoxal 5'-phosphate (PLP)-dependent enzyme, biodegradative arginine decarboxylase (ADC, encoded by AdiA), is a component of an ATR system. The enzyme consumes a cytoplasmic proton in the process of arginine degradation to agmatine. Arginine-agmatine antiporter (AdiC) exchanges the product agmatine for arginine. In this manuscript, we describe the structure of Salmonella typhimurium ADC (StADC). The decameric structure assembled from five dimers related by a non crystallographic 5-fold symmetry represents the first apo-form of the enzyme. The structure suggests that PLP-binding is not a prerequisite for oligomerization. Comparison with E. coli ADC reveals that PLP-binding is accompanied by the movement and ordering of two loops (residues 150-159 and 191-197) and a few active site residues such as His256 and Lys257. A number of residues important for substrate binding are disordered in the apo-StADC structure indicating that PLP binding is important for substrate binding. Unlike the interactions between 5-fold related protomers, interactions that stabilize the dimeric structure are not pH dependent.
PubMed: 28694189
DOI: 10.1016/j.bbrc.2017.07.032
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.7 Å)
構造検証レポート
Validation report summary of 6aa9
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2026-02-04に公開中

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