2hpr

HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR MUTANT WITH MET 51 REPLACED BY VAL AND SER 83 REPLACED BY CYS (M51V, S83C)

spinqualitylabelsall models 2hpr, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2hpr is a 1 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 NonStd Res: CSO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PTHP_BACSU] General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the permease (enzymes II/III). P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity. 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 BACKGROUND: The histidine-containing phosphocarrier protein (HPr) functions in the bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS). His15 on HPr accepts a phosphoryl group from Enzyme I and transfers it to the Enzyme IIA domain of a sugar-specific PTS permease. In addition, HPrs from Gram-positive bacteria undergo phosphorylation on a serine residue, Ser46, which inhibits phosphorylation at His15 and sugar transport. The questions to be addressed at the molecular level are: what is the mechanism of each of the phosphoryl transfers and what conformational transitions are associated with each event? RESULTS: Thus, the crystal structures of the mutants Ser83-->Cys HPr (fully active protein) and Ser46-->Asp HPr (impaired protein which mimics Ser46 approximately P HPr) from Bacillus subtilis have been determined at 2 A resolution. They have been crystallized from high-salt and low-salt solutions respectively, and in two different space groups. Analysis of the two crystal forms reveals some significant differences but these do not alter the overall fold of the protein. In each structure, the side chain of His15 caps the following helix. Two alternative side-chain conformations of Arg17 are observed; it either forms an ion pair with a sulfate ion, presumably resembling the phosphorylated state of the protein (high-salt crystal) or with Glu84 (low-salt crystal). The main-chain conformation in the region of residue 46 is the same in the two crystal forms, with both Ser46 and Asp46 capping the following helix. CONCLUSIONS: The analysis suggests that phosphorylation of either His15 or Ser46 is not associated with main-chain conformational transitions. Rather, the protein is poised to accept the respective phosphoryl group with minor adjustments to side chains. The inhibitory effect of phosphorylation on Ser46 is attributed to the altered surface electrostatics, which impairs protein-protein interaction. Refined structures of the active Ser83-->Cys and impaired Ser46-->Asp histidine-containing phosphocarrier proteins.,Liao DI, Herzberg O Structure. 1994 Dec 15;2(12):1203-16. PMID:7704530 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphocarrier protein

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