5t1o

Solution-state NMR and SAXS structural ensemble of NPr (1-85) in complex with EIN-Ntr (170-424)

spinqualitylabelsall models 5t1o, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5t1o is a 2 chain structure with sequence from Eco57 and Ecoli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: ptsO, Z4569, ECs4085 (ECO57), ptsP, ygdF, ygdO, b2829, JW2797 (ECOLI) Activity: Phosphoenolpyruvate--protein phosphotransferase, with EC number 2.7.3.9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [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). [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). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphocarrier protein HPr 3D structures Phosphotransferase 3D structures

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