1RKU

Crystal Structure of ThrH gene product of Pseudomonas Aeruginosa

1RKU の概要

• エントリーDOI: 10.2210/pdb1rku/pdb
• 関連するPDBエントリー: 1RKV
• 分子名称: homoserine kinase, MAGNESIUM ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: phosphoserine phosphatase, phosphoserine:homoserine phosphotransferase, thrh, phosphoserine phosphoryl donor, transferase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47886.04

構造登録者

Singh, S.K.,Yang, K.,Subramanian, K.,Karthikeyan, S.,Huynh, T.,Zhang, X.,Phillips, M.A.,Zhang, H. (登録日: 2003-11-23, 公開日: 2004-03-30, 最終更新日: 2024-02-14)

主引用文献

Singh, S.K.,Yang, K.,Karthikeyan, S.,Huynh, T.,Zhang, X.,Phillips, M.A.,Zhang, H.
The thrH Gene Product of Pseudomonas aeruginosa Is a Dual Activity Enzyme with a Novel Phosphoserine:Homoserine Phosphotransferase Activity.
J.Biol.Chem., 279:13166-13173, 2004

PubMed Abstract: The thrH gene product of Pseudomonas aeruginosa has been shown to complement both homoserine kinase (thrB gene product) and phosphoserine phosphatase (serB gene product) activities in vivo. Sequence comparison has revealed that ThrH is related to phosphoserine phosphatases (PSP, EC 3.1.3.3) and belongs to the l-2-haloacid dehalogenase-like protein superfamily. We have solved the crystal structures of ThrH in the apoform and in complex with a bound product phosphate. The structure confirms an overall fold similar to that of PSP. Most of the catalytic residues of PSP are also conserved in ThrH, suggesting that similar catalytic mechanisms are used by both enzymes. Spectrophotometry-based in vitro assays show that ThrH is indeed a phosphoserine phosphatase with a K(m) of 0.207 mm and k(cat) of 13.4 min(-1), comparable with those of other PSPs. More interestingly, using high pressure liquid chromatography-based assays, we have demonstrated that ThrH is able to further transfer the phosphoryl group to homoserine using phosphoserine as the phosphoryl group donor, indicating that ThrH has a novel phosphoserine:homoserine phosphotransferase activity.

PubMed: 14699121
DOI: 10.1074/jbc.M311393200

実験手法

X-RAY DIFFRACTION (1.47 Å)