5t1o
From Proteopedia
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| - | ''' | + | {{Large structure}} |
| + | ==Solution-state NMR and SAXS structural ensemble of NPr (1-85) in complex with EIN-Ntr (170-424)== | ||
| + | <StructureSection load='5t1o' size='340' side='right' caption='[[5t1o]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5t1o]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T1O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T1O FirstGlance]. <br> | ||
| + | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate--protein_phosphotransferase Phosphoenolpyruvate--protein phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.9 2.7.3.9] </span></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=5t1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t1o OCA], [http://pdbe.org/5t1o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t1o RCSB], [http://www.ebi.ac.uk/pdbsum/5t1o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t1o ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | {{Large structure}} | ||
| + | == 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). [[http://www.uniprot.org/uniprot/PT1P_ECOLI PT1P_ECOLI]] Component of the phosphoenolpyruvate-dependent nitrogen-metabolic phosphotransferase system (nitrogen-metabolic PTS), that seems to be involved in regulating nitrogen metabolism. Enzyme I-Ntr transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (NPr) (PubMed:10473571). Could function in the transcriptional regulation of sigma-54 dependent operons in conjunction with the NPr (PtsO) and EIIA-Ntr (PtsN) proteins (PubMed:8973315). Enzyme I-Ntr is specific for NPr (PubMed:10473571).<ref>PMID:10473571</ref> <ref>PMID:8973315</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Paralogous enzymes arise from gene duplication events that confer a novel function, although it is unclear how cross-reaction between the original and duplicate protein interaction network is minimized. We investigated HPr:EIsugar and NPr:EINtr, the initial complexes of paralogous phosphorylation cascades involved in sugar import and nitrogen regulation in bacteria, respectively. Although the HPr:EIsugar interaction has been well characterized, involving multiple complexes and transient interactions, the exact nature of the NPr:EINtr complex was unknown. We set out to identify the key features of the interaction by performing binding assays and elucidating the structure of NPr in complex with the phosphorylation domain of EINtr (EINNtr), using a hybrid approach involving X-ray, homology, and sparse nuclear magnetic resonance. We found that the overall fold and active-site structure of the two complexes are conserved in order to maintain productive phosphorylation, however, the interface surface potential differs between the two complexes, which prevents cross-reaction. | ||
| - | + | Structure of the NPr:EINNtr Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems.,Strickland M, Stanley AM, Wang G, Botos I, Schwieters CD, Buchanan SK, Peterkofsky A, Tjandra N Structure. 2016 Dec 6;24(12):2127-2137. doi: 10.1016/j.str.2016.10.007. Epub 2016, Nov 10. PMID:27839951<ref>PMID:27839951</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5t1o" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Phosphoenolpyruvate--protein phosphotransferase]] | ||
| + | [[Category: Buchanan, S]] | ||
| + | [[Category: Peterkofsky, A]] | ||
| + | [[Category: Schwieters, C D]] | ||
| + | [[Category: Stanley, A M]] | ||
| + | [[Category: Strickland, M]] | ||
| + | [[Category: Tjandra, N]] | ||
| + | [[Category: Wang, G]] | ||
| + | [[Category: Bacterial]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Phosphotransfer]] | ||
| + | [[Category: Ptsntr]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 19:34, 9 December 2016
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Solution-state NMR and SAXS structural ensemble of NPr (1-85) in complex with EIN-Ntr (170-424)
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