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| | ==NMR structure of the E. coli protein NPr, residues 1-85== | | ==NMR structure of the E. coli protein NPr, residues 1-85== |
| - | <StructureSection load='5t17' size='340' side='right'caption='[[5t17]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='5t17' size='340' side='right'caption='[[5t17]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5t17]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T17 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T17 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5t17]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T17 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ptsO, Z4569, ECs4085 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5t17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t17 OCA], [http://pdbe.org/5t17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t17 RCSB], [http://www.ebi.ac.uk/pdbsum/5t17 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t17 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5t17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t17 OCA], [https://pdbe.org/5t17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t17 RCSB], [https://www.ebi.ac.uk/pdbsum/5t17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t17 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PTSO_ECO57 PTSO_ECO57]] Component of the phosphoenolpyruvate-dependent nitrogen-metabolic phosphotransferase system (nitrogen-metabolic PTS), that seems to be involved in regulating nitrogen metabolism. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein NPr by enzyme I-Ntr. Phospho-NPr then transfers it to EIIA-Ntr. Could function in the transcriptional regulation of sigma-54 dependent operons in conjunction with the NPr (PtsO) and EIIA-Ntr (PtsN) proteins (By similarity). | + | [https://www.uniprot.org/uniprot/PTSO_ECOLI PTSO_ECOLI] Component of the phosphoenolpyruvate-dependent nitrogen-metabolic phosphotransferase system (nitrogen-metabolic PTS), that seems to be involved in regulating nitrogen metabolism. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein NPr by enzyme I-Ntr. Phospho-NPr then transfers it to EIIA-Ntr. Could function in the transcriptional regulation of sigma-54 dependent operons in conjunction with the NPr (PtsO) and EIIA-Ntr (PtsN) proteins. |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | 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.
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| - | Solution structure of NPr, a bacterial signal-transducing protein that controls the phosphorylation state of the potassium transporter-regulating protein IIA Ntr.,Li X, Peterkofsky A, Wang G Amino Acids. 2008 Oct;35(3):531-9. doi: 10.1007/s00726-008-0079-9. Epub 2008 Apr , 18. PMID:18421563<ref>PMID:18421563</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 5t17" style="background-color:#fffaf0;"></div>
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| | ==See Also== | | ==See Also== |
| | *[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]] | | *[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]] |
| - | == References == | |
| - | <references/> | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Eco57]] | + | [[Category: Escherichia coli O157:H7]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Li, X]] | + | [[Category: Li X]] |
| - | [[Category: Peterkofsky, A]] | + | [[Category: Peterkofsky A]] |
| - | [[Category: Wang, G]] | + | [[Category: Wang G]] |
| - | [[Category: Biofilm]]
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| - | [[Category: Hpr-like]]
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| - | [[Category: Phosphotransfer protein]]
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| - | [[Category: Ptsntr]]
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| - | [[Category: Transferase]]
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