3EZB

COMPLEX OF THE AMINO TERMINAL DOMAIN OF ENZYME I AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI

Replaces:  3EZCReplaces:  3EZD

Summary for 3EZB

• Entry DOI: 10.2210/pdb3ezb/pdb
• Descriptor: PROTEIN (PHOSPHOTRANSFER SYSTEM, ENZYME I), PROTEIN (PHOSPHOCARRIER PROTEIN HPR) (2 entities in total)
• Functional Keywords: phosphotransferase, kinase, sugar transport, transferase
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P08839 P0AA04
• Total number of polymer chains: 2
• Total formula weight: 37510.65

Authors

Clore, G.M.,Garrett, D.S.,Gronenborn, A.M. (deposition date: 1998-11-03, release date: 1999-12-16, Last modification date: 2023-12-27)

Primary citation

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

Experimental method

SOLUTION NMR