3EZE

COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE

3EZE の概要

• エントリーDOI: 10.2210/pdb3eze/pdb
• 分子名称: PROTEIN (PHOSPHOTRANSFERASE SYSTEM, ENZYME I), PROTEIN (PHOSPHOTRANSFERASE SYSTEM, HPR), PHOSPHITE ION (3 entities in total)
• 機能のキーワード: phosphotransferase, transferase, kinase, sugar transport
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm: P08839 P0AA04
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37589.62

構造登録者

Clore, G.M.,Garrett, D.S.,Gronenborn, A.M. (登録日: 1998-11-04, 公開日: 1998-12-16, 最終更新日: 2023-12-27)

主引用文献

Garrett, D.S.,Seok, Y.J.,Peterkofsky, A.,Gronenborn, A.M.,Clore, G.M.
Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr.
Nat.Struct.Biol., 6:166-173, 1999

PubMed Abstract: The solution structure of the first protein-protein complex of the bacterial phosphoenolpyruvate: sugar phosphotransferase system between the N-terminal domain of enzyme I (EIN) and the histidine-containing phosphocarrier protein HPr has been determined by NMR spectroscopy, including the use of residual dipolar couplings that provide long-range structural information. The complex between EIN and HPr is a classical example of surface complementarity, involving an essentially all helical interface, comprising helices 2, 2', 3 and 4 of the alpha-subdomain of EIN and helices 1 and 2 of HPr, that requires virtually no changes in conformation of the components relative to that in their respective free states. The specificity of the complex is dependent on the correct placement of both van der Waals and electrostatic contacts. The transition state can be formed with minimal changes in overall conformation, and is stabilized in favor of phosphorylated HPr, thereby accounting for the directionality of phosphoryl transfer.

PubMed: 10048929
DOI: 10.1038/5854

実験手法

SOLUTION NMR