2HPR
HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR MUTANT WITH MET 51 REPLACED BY VAL AND SER 83 REPLACED BY CYS (M51V, S83C)
Summary for 2HPR
Entry DOI | 10.2210/pdb2hpr/pdb |
Descriptor | HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR, SULFATE ION (3 entities in total) |
Functional Keywords | phosphotransferase |
Biological source | Bacillus subtilis |
Cellular location | Cytoplasm: P08877 |
Total number of polymer chains | 1 |
Total formula weight | 9163.20 |
Authors | Herzberg, O. (deposition date: 1992-09-09, release date: 1993-01-15, Last modification date: 2024-10-23) |
Primary citation | Liao, D.I.,Herzberg, O. Refined structures of the active Ser83-->Cys and impaired Ser46-->Asp histidine-containing phosphocarrier proteins. Structure, 2:1203-1216, 1994 Cited by PubMed Abstract: 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? PubMed: 7704530DOI: 10.1016/S0969-2126(94)00122-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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