Phosphocarrier protein

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Revision as of 08:35, 17 November 2019

spinqualitylabelsall models Structure of phosphocarrier protein HPr (PDB entry 1fu0) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Phosphocarrier protein HPr (HPr) is a component of the sugar phosphotransferase system. The system catalyses the phosphorylation of sugars during their translocation across cell membrane. A phosphoryl group is transferred from phosphoenolpyruvate via several enzymes (EI, EII) to HPr[1]. A conserved histidine in the N terminal of HPr is the acceptor of the phosphate. In Gram-positive bacteria HPr there is a conserved serine which is phosphorylated. Phosphocarrier protein NPr (NPr) is a component of the sugar phosphotransferase system. NPr is a phosphoryl transfer protein, homologous to HPr which functions to regulate nitrogen metabolism[2]. Phosphocarrier protein III Glc (PcpIII) is a signal-transducing component of the phosphoenolpyruvate:glycose phosphotransferase system of E. coli[3]. Structural highlights The prohibits the HPr to act as a phosphocarrier in the EI reaction[4]. 3D structures of phosphocarrier protein HPr Phosphocarrier protein HPr 3D structures

3D structures of phosphocarrier protein HPr

Updated on 17-November-2019

References

1. ↑ Postma PW, Lengeler JW, Jacobson GR. Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. Microbiol Rev. 1993 Sep;57(3):543-94. PMID:8246840
2. ↑ 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. 2008 Oct;35(3):531-9. doi: 10.1007/s00726-008-0079-9. Epub 2008 Apr , 18. PMID:18421563 doi:http://dx.doi.org/10.1007/s00726-008-0079-9
3. ↑ Maurer T, Doker R, Gorler A, Hengstenberg W, Kalbitzer HR. Three-dimensional structure of the histidine-containing phosphocarrier protein (HPr) from Enterococcus faecalis in solution. Eur J Biochem. 2001 Feb;268(3):635-44. PMID:11168402
4. ↑ Audette GF, Engelmann R, Hengstenberg W, Deutscher J, Hayakawa K, Quail JW, Delbaere LT. The 1.9 A resolution structure of phospho-serine 46 HPr from Enterococcus faecalis. J Mol Biol. 2000 Nov 3;303(4):545-53. PMID:11054290 doi:10.1006/jmbi.2000.4166