1SPH

REFINED STRUCTURES OF THE ACTIVE S83C AND IMPAIRED S46D HPRS: EVIDENCE THAT PHOSPHORYLATION DOES NOT REQUIRE A BACKBONE CONFORMATIONAL TRANSITION

Summary for 1SPH

• Entry DOI: 10.2210/pdb1sph/pdb
• Descriptor: HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR (2 entities in total)
• Functional Keywords: phosphotransferase
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 18452.69

Authors

Liao, D.-I.,Herzberg, O. (deposition date: 1994-11-03, release date: 1995-02-07, Last modification date: 2024-02-14)

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

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: 7704530
DOI: 10.1016/S0969-2126(94)00122-7

Experimental method

X-RAY DIFFRACTION (2 Å)