5T17
NMR structure of the E. coli protein NPr, residues 1-85
Summary for 5T17
| Entry DOI | 10.2210/pdb5t17/pdb |
| NMR Information | BMRB: 30157 |
| Descriptor | Phosphocarrier protein NPr (1 entity in total) |
| Functional Keywords | ptsntr, phosphotransfer protein, hpr-like, biofilm, transferase |
| Biological source | Escherichia coli O157:H7 |
| Total number of polymer chains | 1 |
| Total formula weight | 9254.57 |
| Authors | Wang, G.,Li, X.,Peterkofsky, A. (deposition date: 2016-08-18, release date: 2016-09-28, Last modification date: 2024-05-01) |
| Primary citation | 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 Cited by 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: 18421563DOI: 10.1007/s00726-008-0079-9 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
