Phosphocarrier protein
From Proteopedia
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| - | <StructureSection load=' | + | <StructureSection load='' size='350' side='right' caption='Structure of phosphocarrier protein HPr (PDB entry [[1fu0]])' scene='57/570591/Cv/1'> |
== Function == | == 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<ref>PMID:8246840</ref>. 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 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<ref>PMID:8246840</ref>. 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. | ||
Revision as of 15:07, 31 August 2017
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3D structures of phosphocarrier protein HPr
Updated on 31-August-2017
References
- ↑ Postma PW, Lengeler JW, Jacobson GR. Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. Microbiol Rev. 1993 Sep;57(3):543-94. PMID:8246840
- ↑ 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
- ↑ 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
- ↑ 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
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