5T17

NMR structure of the E. coli protein NPr, residues 1-85

5T17 の概要

• エントリーDOI: 10.2210/pdb5t17/pdb
• NMR情報: BMRB: 30157
• 分子名称: Phosphocarrier protein NPr (1 entity in total)
• 機能のキーワード: ptsntr, phosphotransfer protein, hpr-like, biofilm, transferase
• 由来する生物種: Escherichia coli O157:H7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9254.57

構造登録者

Wang, G.,Li, X.,Peterkofsky, A. (登録日: 2016-08-18, 公開日: 2016-09-28, 最終更新日: 2024-05-01)

主引用文献

Li, X.,Peterkofsky, A.,Wang, G.
Solution structure of NPr, a bacterial signal-transducing protein that controls the phosphorylation state of the potassium transporter-regulating protein IIA Ntr.
Amino Acids, 35:531-539, 2008

PubMed Abstract: A nitrogen-related signal transduction pathway, consisting of the three phosphotransfer proteins EI(Ntr), NPr, and IIA(Ntr), was discovered recently to regulate the uptake of K(+) in Escherichia coli. In particular, dephosphorylated IIA(Ntr) inhibits the activity of the K(+) transporter TrkA. Since the phosphorylation state of IIA(Ntr) is partially determined by its reversible phosphorylation by NPr, we have determined the three-dimensional structure of NPr by solution NMR spectroscopy. In total, we obtained 973 NOE-derived distance restraints, 112 chemical shift-derived backbone angle restraints, and 35 hydrogen-bond restraints derived from temperature coefficients (wave). We propose that temperature wave is useful for identifying exposed beta-strands and assists in establishing protein folds based on chemical shifts. The deduced structure of NPr contains three alpha-helices and four beta-strands with the three helices all packed on the same face of the beta-sheet. The active site residue His16 of NPr for phosphoryl transfer was found to be neutral and in the N epsilon 2-H tautomeric state. There appears to be increased motion in the active site region of NPr compared to HPr, a homologous protein involved in the uptake and regulation of carbohydrate utilization.

PubMed: 18421563
DOI: 10.1007/s00726-008-0079-9

実験手法

SOLUTION NMR