1SPH

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

1SPH の概要

• エントリーDOI: 10.2210/pdb1sph/pdb
• 分子名称: HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR (2 entities in total)
• 機能のキーワード: phosphotransferase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18452.69

構造登録者

Liao, D.-I.,Herzberg, O. (登録日: 1994-11-03, 公開日: 1995-02-07, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)