1POH

THE 2.0 ANGSTROMS RESOLUTION STRUCTURE OF ESCHERICHIA COLI HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR: A REDETERMINATION

1POH の概要

• エントリーDOI: 10.2210/pdb1poh/pdb
• 分子名称: HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR, SULFATE ION (3 entities in total)
• 機能のキーワード: phosphotransferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9321.46

構造登録者

Jia, Z.,Quail, W.,Delbaere, L. (登録日: 1993-10-19, 公開日: 1994-01-31, 最終更新日: 2024-02-14)

主引用文献

Jia, Z.,Quail, J.W.,Waygood, E.B.,Delbaere, L.T.
The 2.0-A resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. A redetermination.
J.Biol.Chem., 268:22490-22501, 1993

PubMed Abstract: The x-ray structure of Escherichia coli HPr has been redetermined at 2.0-A resolution. In contrast to the previous study (El-Kabbani, O. A. L., Waygood, E. B., and Delbaere, L. T. J. (1987) J. Biol. Chem. 262, 12926-12929), the overall structure is, in general, similar to other reported NMR and x-ray HPr structures, although there are some important differences in detail. The overall folding topology of HPr is a classical open-faced beta-sandwich, consisting of four antiparallel beta-strands and three alpha-helices. The least square refinement produced an R index of 0.135 for all measured unique data between 8.0 and 2.0 A resolution. The active center consists of His15 which is hydrogen bonded to a sulfate anion, and Arg17 which has a fully open conformation. This corresponds to the first observed "semi-closed" conformation of the active center of HPr. The Streptococcus faecalis HPr structure (Jia, Z., Vandonselaar, M., Quail, J. W., and Delbaere, L. T. J. (1993) Nature 361, 94-97) has the "open" conformation in which the side chains of His15 and Arg17 are directed as far away from each other as possible. The Bacillus subtilis HPr (Herzberg, O., Reddy, P., Sutrina, S., Saier, M. H., Jr., Reizer, J., and Kapadia, G. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 2499-2503) has the "closed" conformation in which the side chains of His15 and Arg17 are close together with a sulfate anion located in the active center. The open conformation represents the unphosphorylated form of HPr whereas the closed conformation likely resembles the phosphorylated form of HPr. The semi-closed conformation observed in the E. coli HPr structure could represent a structural intermediate on the phosphorylation/dephosphorylation pathway of HPr.

PubMed: 8226757

実験手法

X-RAY DIFFRACTION (2 Å)