1a6j | pdb_00001a6j

NITROGEN REGULATORY BACTERIAL PROTEIN IIA-NITROGEN

spinqualitylabelsall models 1a6j, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1a6j is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BME, SO4 Activity: Protein-N(pi)-phosphohistidine--sugar phosphotransferase, with EC number 2.7.1.69 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PTSN_ECOLI] Seems to have a role in regulating nitrogen assimilation (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The bacterial rpoN operon codes for sigma 54, which is the key sigma factor that, under nitrogen starvation conditions, activates the transcription of genes needed to assimilate ammonia and glutamate. The rpoN operon contains several other open reading frames that are cotranscribed with sigma 54. The product of one of these, the 17.9 kDa protein IIANtr, is homologous to IIA proteins of the phosphoenolpyruvate:sugar phosphotransferase (PTS) system. IIANtr influences the transcription of sigma 54-dependent genes through an unknown mechanism and may thereby provide a regulatory link between carbon and nitrogen metabolism. Here we describe the 2.35 A X-ray structure of Escherichia coli IIANtr. It is the first structure of a IIA enzyme from the fructose-mannitol family of the PTS. The enzyme displays a novel fold characterized by a central mixed parallel/anti-parallel beta-sheet surrounded by six alpha-helices. The active site His73 is situated in a shallow depression on the protein surface. The three-dimensional structure of the nitrogen regulatory protein IIANtr from Escherichia coli.,Bordo D, van Monfort RL, Pijning T, Kalk KH, Reizer J, Saier MH Jr, Dijkstra BW J Mol Biol. 1998 May 29;279(1):245-55. PMID:9636714 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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