| 词条 | Phosphocarrier protein |
| 释义 |
| Symbol = PTS_HPr_protein | Name = Phosphotransferase system, phosphocarrier HPr protein | image = 1poh.jpg | width = 270 | caption = Phosphocarrier protein HPr, E.Coli | Pfam = PF00381 | InterPro = IPR000032 | SMART = | PROSITE = PDOC00318 | SCOP = 1ptf | PDB = {{PDB2|1cm2}}, {{PDB2|1cm3}}, {{PDB2|1fu0}}, {{PDB2|1ggr}}, {{PDB2|1hdn}}, {{PDB2|1j6t}}, {{PDB2|1jem}}, {{PDB2|1k1c}}, {{PDB2|1ka5}}, {{PDB2|1kkl}} }}Phosphocarrier HPr protein is a small cytoplasmic protein that is a component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS).[1][2] The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) is a major carbohydrate transport system in bacteria. The PTS catalyses the phosphorylation of sugar substrates during their translocation across the cell membrane. The mechanism involves the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) via enzyme I (EI) to enzyme II (EII) of the PTS system, which in turn transfers it to a phosphocarrier protein (HPr).[3][4] In some bacteria HPr is a domain in a larger protein that includes an EIII(Fru) (IIA) domain and in some cases also an EI domain. There is a conserved histidine in the N-terminus of HPr, which serves as an acceptor for the phosphoryl group of EI. In the central part of HPr there is a conserved serine which, in Gram-positive bacteria only, is phosphorylated by an ATP-dependent protein kinase, a process which probably plays a regulatory role in sugar transport. References1. ^{{cite journal |vauthors=Postma PW, Lengeler JW, Jacobson GR |title=Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria |journal=Microbiol. Rev. |volume=57 |issue=3 |pages=543–594 |year=1993 |pmid=8246840 |pmc=372926}} {{InterPro content|IPR000032}}2. ^{{cite journal |vauthors=Meadow ND, Fox DK, Roseman S |title=The bacterial phosphoenolpyruvate: glycose phosphotransferase system |journal=Annu. Rev. Biochem. |volume=59 |issue=1|pages=497–542 |year=1990 |pmid=2197982 |doi=10.1146/annurev.bi.59.070190.002433}} 3. ^{{cite journal |vauthors=Boelens R, Scheek RM, Robillard GT, van Nuland NA |title=High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data |journal=J. Mol. Biol. |volume=246 |issue=1 |pages=180–193 |year=1995 |pmid=7853396 |doi=10.1006/jmbi.1994.0075}} 4. ^{{cite journal |doi=10.1016/S0969-2126(94)00122-7 |vauthors=Liao DI, Herzberg O |title=Refined structures of the active Ser83→Cys and impaired Ser46→Asp histidine-containing phosphocarrier proteins |journal=Structure |volume=2 |issue=12 |pages=1203–1216 |year=1994 |pmid=7704530}} 1 : Protein families |
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